No matter how high the energy, the little negative particles won't break apart. But that doesn't mean they are indestructible.

Using several massive supercomputers, a team of physicists has split a simulated electron perfectly in half. The results, which were published in the Jan. 13 issue of Science, are another example of how tabletop experiments on ultra-cold atoms and other condensed-matter materials can provide clues about the behavior of fundamental particles.

In the simulations, Duke University physicist Matthew Hastings and his colleagues, Sergei Isakov of the University of Zurich and Roger Melko of the University of Waterloo in Canada, developed a virtual crystal. Under extremely low temperatures in the computer model, the crystal turned into a quantum fluid, an exotic state of matter where electrons begin to condense.

Many different types of materials, from superconductors to superfluids, can form as electrons condense and are chilled close to absolute zero, about -459 degrees Fahrenheit. That's approximately the temperature at which particles simply stop moving. It's also the temperature region where individual particles, such as electrons, can overcome their repulsion for each other and cooperate.

The cooperating particles' behavior eventually becomes indistinguishable from the actions of an individual. Hastings says the phenomenon is a lot like what happens with sound. A sound is made of sound waves. Each sound wave seems to be indivisible and to act a lot like a fundamental particle. But a sound wave is actually the collective motion of many atoms, he says.

Under ultra-cold conditions, electrons take on the same type of appearance. Their collective motion is just like the movement of an individual particle. But, unlike sound waves, cooperating electrons and other particles, called collective excitations or quasiparticles, can "do things that you wouldn't think possible," Hastings says.

The quasiparticles formed in this simulation show what happens if a fundamental particle were busted up, so an electron can't be physically smashed into anything smaller, but it can be broken up metaphorically, Hastings says.

He and his colleagues divided one up by placing a virtual particle with the fundamental charge of an electron into their simulated quantum fluid. Under the conditions, the particle fractured into two pieces, each of which took on one-half of the original's negative charge.

As the physicists continued to observe the new sub-particles and change the constraints of the simulated environment, they were also able to measure several universal numbers that characterize the motions of the electron fragments. The results provide scientists with information to look for signatures of electron pieces in other simulations, experiments and theoretical studies.

Successfully simulating an electron split also suggests that physicists don't necessarily have to smash matter open to see what's inside; instead, there could be other ways to coax a particle to reveal itself.

Source: ScienceDaily - via ZeitNews.org

Assessing these benefits to populations in ways that are useful to decisionmakers who guide conservation efforts has, however, proved difficult.

A global analysis published in the January 2012 issue of BioScience by Will R. Turner of Conservation International and his colleagues breaks new ground by analyzing the flow of benefits from ecosystem services under a variety of socioeconomic assumptions and in greater spatial detail than previous studies. The analysis, which divides the globe into more than 58,000 hexagons, finds that over half the global value of ecosystem services benefitting the world's poorest people originates in areas that are a high priority for conservation. Moreover, the value of ecosystem services generated by the top quarter of biodiversity sites is more than triple the effective cost of conserving them.

If there were effective and equitable mechanisms to ensure that the beneficiaries of ecosystem services paid those responsible for stewarding them, Turner and his colleagues conclude, global benefits to poor communities would robustly increase by 50 percent, and the payments would amount to more than a dollar per person per day for about a third of the 1.1 billion people in the world living in dire poverty. The authors say their findings reinforce the idea that there is an important concordance between biodiversity, provision of ecosystem services, and poverty that policymakers could use in designing equitable payment schemes to address both poverty and loss of biodiversity.

Source: EurekAlert - via ZeitNews.org

For example, when you log in to your online bank account, signcryption prevents your username and password from being seen by unauthorized individuals. At the same time, it confirms your identity for the bank.

UNC Charlotte professor Yuliang Zheng invented the revolutionary new technology and he continues his research in the College of Computing and Informatics. After nearly a three-year process, his research efforts have been formally recognized as an international standard by the International Organization of Standardization (ISO).

News of the ISO adoption comes amidst daily reports of cyber attack and cyber crime around the world. Zheng says the application will also enhance the security and privacy of cloud computing.

“The adoption of signryption as an international standard is significant in several ways,” he said. “It will now be the standard worldwide for protecting confidentiality and authenticity during transmissions of digital information.”

Known as the father of the signcryption technology, Zheng is internationally recognized as an authority in cryptography and network security. He has published more than 200 scholarly articles and books on security and holds several patents in cyber security. His most recent publication “Practical Signcryption” is currently on sale worldwide.

“This will also allow smaller devices, such as smartphones and PDAs, 3G and 4G mobile communications, as well as emerging technologies, such as radio frequency identifiers (RFID) and wireless sensor networks, to perform high-level security functions,” he said. “And, by performing these two functions simultaneously, we can save resources, be it an individual’s time or be it energy, as it will take less time to perform the task.”

Source: PhysOrg - via ZeitNews.org

Do you feel differently depending on whether your co-worker is a man or a woman? According to a new study, workers who witness incivility towards colleagues feel negative emotions – especially when the incivility is aimed at workers of the same sex. The work, by Kathi Miner from Texas A&M University and Angela Eischeid from Buena Vista University, Iowa, is the first to look at the relationship between employees' observations of incivility towards same gender co-workers and negative emotions. It is published online in Springer's journal Sex Roles.

Workplace incivility is commonplace and violates conventional workplace norms for mutual respect. It also displays a lack of regard for others. Although our first thoughts are likely to be for the victim of this 'abuse', it can also affect our own feelings as observers.

Miner and Eischeid examined how observed workplace incivility towards female and male co-workers relates to four negative emotions - anger, demoralization, fear and anxiety - for both female and male observers. A total of 453 restaurant employees responded to an online survey examining the 'quality of life in the restaurant industry'.

Analyses showed that female observers reported significantly higher levels of anger, demoralization, fear and anxiety the more they observed other female employees being treated rudely and discourteously at work, in comparison to male employees. Demoralization was the strongest negative emotion experienced by observing women.

Similarly, male observers were significantly more angry, fearful and anxious the more they observed other men being treated uncivilly at work, compared to females. Interestingly, demoralization was not a negative emotion experienced by male observers in these situations.

The authors conclude: "Our results paint a complex picture about the experience of specific negative emotions in response to observed incivility toward same gender co-workers. In some cases, women are more affected (demoralized) and in others, men are more affected (angry, fearful and anxious). In both cases, witnessing incivility towards same gender co-workers can have significant affective consequences for observers."

Source: EurekAlert

This opens up new implications for the treatment of neurological and psychiatric conditions, even suggesting that diet choices might influence their progression.

In spite of more than 20 years of research efforts, the enzymatic function of the CRYM protein has remained elusive. Previous research has shown that CRYM functions both as an important structural protein and a binder of thyroid hormones, but PhD student Andre Hallen suspected something more.

"CRYM was first discovered in the ocular lens of marsupials, that is, in Skippy's eye! Since then, we've seen it in lamb brains, in other tissues and learnt how it can be observed and mutated in mammals like humans. Now we can see more of its full potential in human health and nutrition," Hallen explains.

In a study published in the Journal of Neurochemistry, Hallen conclusively demonstrated an enzyme function for CRYM, and identified how this enzymatic activity reveals a new role for thyroid hormones in regulating mammalian amino acid metabolism.

It also recognises a possible reciprocal role of enzyme activity in regulating bioavailability of intracellular T3, with further research pathways for how this regulatory role might open up new treatment options for a range of neurological and psychiatric conditions.

Hallen lead a team of scientists on this study, including three months working in North America with Dr Arthur Cooper, a world authority on neurochemistry and amino acid chemistry.

His research has also sparked the interest of international scientists, including Patrick W Reed and Robert J Bloch of the University of Maryland, who profiled Hallen's work in their article ‘Crystallin-Gazing: Unveiling Enzymatic Activity'.

In 2012, Hallen will continue his research into this area, further exploring the role of diet in influencing hormone function, and the effects of these changes on the CRYM protein, its related mutations and conditions.

Source: Macquarie University - via ZeitNews.org

Although you may never have seen it happen yourself, it isn't all that uncommon for large objects - including people - to fall onto the tracks at subway or railway platforms. While security personnel viewing CCTV feeds will catch some of these accidents, the cameras' shots are sometimes obscured by people, poor lighting, or even the trains themselves. The results can range from lengthy delays in rail service, to fatalities. Now, however, researchers working on a project for the Université Lille Nord de France have developed a system that uses radar to automatically detect and identify objects that fall onto the tracks. When installed at a platform, the system could then shut off power to the tracks, and notify oncoming trains.

The system continuously sends out wideband radio waves, and analyzes their reflections when they're bounced back by a foreign object, via an Automatic Target Recognition procedure. Only the most prominent features of the object's reflected signal are processed, and then compared to a database of known objects.

In a computer simulation, the researchers tested the system using objects such as suitcases, bottles, and the bodies of human adults, adolescents and children. In all cases, it was able to accurately identify the objects. Physical tests were also conducted in an echo-free chamber, in which the radio waves were guided towards two men, a woman, and two pieces of luggage made of different materials. Once again, it was able to differentiate between the subjects.

"We hope these devices will be used in the near future since they are very complementary to existing video systems and have a similar final cost," said Ali Mroué, lead author of a paper on the research. "The complementary use of video and radar systems could lead to low levels of false detection, which is mandatory for this application, and maximize the chance of survival for passengers who have fallen on the line."

Source: GizMag - via zeitnews.org

Add one more data point to the decades-old debate over marijuana legalization: A new study concludes that casual pot smoking - up to one joint per day - does not affect the functioning of your lungs.

The study, published in the Jan. 11, 2012 edition of Journal of the American Medical Association, also offered up a nugget that likely will surprise many: Evidence points to slight increases in lung airflow rates and increases in lung volume from occasional marijuana use.

Air flow is the amount of air someone can blow out of their lungs one second after taking the deepest breath possible. The volume measure is the total amount of air blown out once someone has taken the deepest breath possible.

Association Between Marijuana Exposure and Pulmonary Function Over 20 Years

The study of 5115 men and women took place over two decades between March 26, 1985 and August 19, 2006 in 4 American cities: Birmingham, Chicago, Oakland, Calif., and Minneapolis.

"With marijuana use increasing and large numbers of people who have been and continue to be exposed, knowing whether it causes lasting damage to lung function is important for public-health messaging and medical use of marijuana," according to one of the study's co-authors, Stefan Kertesz. "At levels of marijuana exposure commonly seen in Americans, occasional marijuana use was associated with increases in lung air flow rates and increases in lung capacity."

He added that those increases, though not large, nonetheless were statistically significant. "And the data showed that even up to moderately high-use levels -- one joint a day for seven years -- there is no evidence of decreased air-flow rates or lung volumes," he said.

The study by researchers at the University of California, San Francisco, and the University of Alabama at Birmingham was released Tuesday by the Journal of the American Medical Association.

Echo of past findings

The findings echo results in some smaller studies that showed while marijuana contains some of the same toxic chemicals as tobacco, it does not carry the same risks for lung disease. It's not clear why that is so, but it's possible that the main active ingredient in marijuana, a chemical known as THC, makes the difference. THC causes the "high" that users feel. It also helps fight inflammation and may counteract the effects of more irritating chemicals in the drug, said Dr. Donald Tashkin, a marijuana researcher and an emeritus professor of medicine at the University of California, Los Angeles. Tashkin was not involved in the new study.

Study co-author Dr. Stefan Kertesz said there are other aspects of marijuana that may help explain the results.

Unlike cigarette smokers, marijuana users tend to breathe in deeply when they inhale a joint, which some researchers think might strengthen lung tissue. But the common lung function tests used in the study require the same kind of deep breathing that marijuana smokers are used to, so their good test results might partly reflect lots of practice, said Kertesz, a drug abuse researcher and preventive medicine specialist at the Alabama university.

Roughly equal numbers of blacks and whites took part, but no other minorities. Participants were periodically asked about recent marijuana or cigarette use and had several lung function tests during the study.

Overall, about 37 percent reported at least occasional marijuana use, and most users also reported having smoked cigarettes; 17 percent of participants said they'd smoked cigarettes but not marijuana. Those results are similar to national estimates.

On average, cigarette users smoked about 9 cigarettes daily, while average marijuana use was only a joint or two a few times a month -- typical for U.S. marijuana users, Kertesz said.

The authors calculated the effects of tobacco and marijuana separately, both in people who used only one or the other, and in people who used both. They also considered other factors that could influence lung function, including air pollution in cities studied.

The analyses showed pot didn't appear to harm lung function, but cigarettes did. Cigarette smokers' test scores worsened steadily during the study. Smoking marijuana as often as one joint daily for seven years, or one joint weekly for 20 years was not linked with worse scores. Very few study participants smoked more often than that.

Like cigarette smokers, marijuana users can develop throat irritation and coughs, but the study didn't focus on those. It also didn't examine lung cancer, but other studies haven't found any definitive link between marijuana use and cancer.

Source: © 2012 CBS Interactive Inc. All Rights Reserved.

Most research has focused on using batteries, tiny solar cells or piezoelectric generators to harvest kinetic energy from the movement of an insect's wings to power the electronics attached to the insects. Now a group of researchers at Case Western Reserve University have created a power supply that relies just on the insect's normal feeding.

Recognizing that using a real insect is much easier than starting from scratch to create a device that works like an insect, Case Western Reserve chemistry professor teamed up with graduate student Michelle Rasmussen, biology professor Roy E. Ritzmann, chemistry professor Irene Lee and biology research assistant Alan J. Pollack to develop an implantable biofuel cell to provide usable power for the various sensors, recording devices, or electronics used to control an insect cyborg.

To convert chemical energy harvested from the insect and turn it into electricity, the team used two enzymes in series to create the anode. The first enzyme breaks down the sugar trehalose, which a cockroach constantly produces from its food, into two simpler sugars, called monosaccarides, while the second enzyme oxidizes the monosaccarides to release electrons. A current them flows as the electrons are drawn to the cathode, where oxygen from air takes up the electrons and is reduced to water.

After testing the system using trehalose solution, the team inserted prototype electrodes in a blood sinus away from critical organs in the abdomen of a female cockroach. The cockroaches suffered no long-term damage, which the researchers say bodes well for long-term use.

"Insects have an open circulatory system so the blood is not under much pressure," Ritzmann explained. "So, unlike say a vertebrate, where if you pushed a probe into a vein or worse an artery (which is very high pressure) blood does not come out at any pressure. So, basically, this is really pretty benign. In fact, it is not unusual for the insect to right itself and walk or run away afterward."

Using an instrument called a potentiostat, the team determined the maximum power density of the fuel cell reached nearly 100 microwatts per square centimeter at 0.2 volts, with a maximum current density of about 450 microamps per square centimeter.

The researchers are now working to miniaturize the fuel cell so that it can be fully implanted into an insect while still allowing it to run or fly normally and examining which materials might last for a long time inside an insect. They are also working with other researchers to develop a signal transmitter that can run on little energy and also exploring how to add a lightweight rechargeable battery to the system.

"It's possible the system could be used intermittently," Scherson said. "An insect equipped with a sensor could measure the amount of noxious gas in a room, broadcast the finding, shut down and recharge for an hour, then take a new measurement and broadcast again."

Source: GIZMAG - via ZeitNews.org

David Forbes was on his way home to Tucson, Arizona, after a family trip last summer when a policeman stopped him in the Detroit airport. The officer said he had received 50 panicked phone calls since Forbes had entered the building, and now his entire family had been marked for extra screening. The delay was inconvenient, but it shouldn’t have come as a surprise. Forbes had 160 circuit boards and enough electronics to start a data center strapped to his body. What the authorities didn’t realize, though, was that all the equipment wasn’t dangerous—it was actually a wearable TV set.

Forbes, an electrical engineer, built his first video coat in 2009 after getting his hands on a collection of surplus LED displays. He transformed them into what he calls “the world’s worst television,” an all-red screen that weighed 50 pounds. He wanted to make a better, lighter version, and thanks to a side business selling homemade wristwatches, he had the spare cash. He laid an old overcoat out on a table, measured its dimensions, and guessed that he could fit it with enough LEDs to create a sharp 160-by-120-pixel display. Next he sorted through his gadget box and found a few flexible circuit boards. The flexibility was ideal for a wearable screen, but he wanted to have more pixels, so he built a prototype of a long, thin board with 30 rows of four LEDs each and shipped it to a circuit-board manufacturer to make 175 more.

Screen Shot: When the vest is displaying video, roughly five gigabits of data flows to the LEDs every second.  Steven Meckler

Forbes also built an additional circuit board to scale down the analog video signal from his iPod, and three other circuit boards that translate the signals into instructions for the LEDs and deliver power from two lithium-polymer batteries. He put the batteries into his pants pockets, and hot-glued the control boards to the shoulders and the flexible display boards to the front and back of the coat. A little Velcro down the middle replaced the buttons on the coat. The finished version weighed only eight pounds.

At the airport, Forbes convinced airport security that he wasn’t a threat by offering to show them The Simpsons on the coat. Since then, he has cut the coat into two less-cumbersome vests. Although they’re relatively comfortable and they work well, they haven’t replaced his family TV. “I’m not using them daily,” he says, “but they get taken out now and then if I’m in the mood for a little attention from strangers.”

Image Generation: The iPod connects to a circuit board that has a chip normally used to scale down the pixels in surveillance video. Steven Meckler

How It Works

Time: 6 months

Cost: $20,000

DISPLAY

Forbes’s iPod plugs into a circuit board on the vest’s left shoulder. The board includes a digitizing chip—a type used in security video systems that allows the feeds from four cameras to fit on one monitor—that he repurposed to scale iPod video down to a resolution consistent with his display. Additional processing converts the iPod data into signals for the LEDs, which travel along Ethernet-like cables to four separate boards, one on each shoulder and hip. From there, the signals move through ribbon cables to the three miniature chips on each of the flexible circuit boards located on the chest and back. The chips turn the LEDs on and off 360 times a second to create the illusion of changing color and brightness.

POWER

Heavy batteries would make the coat hard to wear, so Forbes found an R/C hobby shop in Washington that sold lightweight, inexpensive lithium-polymer batteries. One battery fit in each pocket, which gave the coat roughly an hour of run-time. The smaller vests last up to 90 minutes.

AUDIO

Forbes initially thought about rigging small speakers to the shoulders of the coat, but he realized that they wouldn’t be powerful enough to let him show off his invention at Burning Man, the annual festival in the Nevada desert. So he wired the coat to another one of his inventions, a boom box for bicycles that he built from a six-inch-diameter drain pipe and a pair of outdoor marine speakers.

Source: PopSci - via ZeitNews.org

The protein is an enzyme that Plasmodium falciparum, the protozoan that causes the most lethal form of malaria, uses to make cell membrane.

The protozoan cannot survive without this enzyme, but even though the enzyme has many lookalikes in other organisms, people do not make it. Together these characteristics make the enzyme an ideal target for new antimalarial drugs.

The research was published in the January 6 issue of the Journal of Biological Chemistry (JBC) as "Paper of the Week" for that issue.

A cartoon based on the electron density map makes it easier to see the protein’s structure and figure out how it works. The enzyme’s job is to add a methyl group — three times — to a starting molecule as part of a process for making cell membranes. In this cartoon, the phosphate is a stand-in for the starting molecule and the green molecule is the one that donates a methyl group. Both are positioned in the active site of the enzyme, the pocket where the chemistry takes place.

The work also will be featured in ASBMB Today (the newsletter of the American Society for Biological Molecular Biology, which publishes JBC), and it will be the topic of a JBC podcast.

Sweating the cold room

The protein's structure might have remained an enigma, had it not been the "unreasonable optimism" of Joseph Jez, PhD, associate professor of biology in Arts & Sciences, which carried his team through a six-year-long obstacle course of failures and setbacks.

"What my lab does is crystallize proteins so that we can see what they look like in three dimensions," Jez says. "The idea is that if we know a protein's structure, it will be easier to design chemicals that would target the protein's active site and shut it down," Jez says.

The lastest discovery is the culmination of a project that began years before when Jez was working at the Danforth Plant Science Center in St. Louis and collaborating with scientists at the local biotech startup Divergence.

"At the time, C. elegans had just been sequenced and the Divergence scientists were looking at using it as an easy model to work out the biochemistry of parasitic nematodes," Jez says.

C. elegans is a free-living nematode, or microscopic roundworm, but many nematodes are parasitic and cause disease in plants, livestock and people.

During this project, Lavanya Palavalli, a summer intern working with Jez, crystallized the C. elegans version of the enzyme. The job of the enzyme, phosphoethanolamine methyltransferase, thankfully abbreviated to PMT, is to add methyl groups to a starting molecule, phosophoethanolamine.

"When Soon Goo Lee later took up the project," says Jez, "the plan was to try to grow better crystals of the C. elegans protein, ones good enough to get readable X-ray diffraction patterns.

Two years later, the crystals were looking better but still not good enough.

So Jez suggested that Lee go after homologous (look-alike) proteins in other organisms. "Even though the proteins are homologous, each has a different amino acid sequence and so will behave differently in the crystallizations," Jez says. "Lee went from working with two C. elegans proteins to three plant proteins, two other nematode proteins and then the Plasmodium protein," Jez says.

"He took all six of those PMT versions into the crystallization trials to maximize his odds," Jez says.

"To crystallize a protein," Jez says, "we put a solution of a salt or something else that might work as a desiccant in the bottom of a small well. And then we put a drop of our liquid protein on a microscope cover slip and flip it over the top of the well, so the drop of protein is hanging upside down in the well."

"What we're trying to do is to slowly withdraw water from the protein. It's exactly like making rock candy, only in that case, the string hanging into the jar of sugar solution helps to withdraw water," he says.

The difference is that sugar wants to form crystals and proteins are reluctant to do so.

"There are 24 wells to a tray, and we usually screen 500 wells per protein at first," Jez says. "Lee had eight proteins and so his first pass was to screen 4,000 conditions. And then he had to try different combinations of ligands to the proteins and crystallize those. This is why it took a few years to finally get where he needed to go."

Road trip!

The scientists need crystals — preferably nice, big ones —to stick in the path of an X-ray beam at Argonne National Laboratory in Chicago. (If the crystal is a good one, and all the atoms are lined up in a repeating array, the scattered X-rays will produce a clear pattern of spots.)

Soon Goo Lee, a doctoral candidate at Washington University in St. Louis, about to click the mouse button to see whether six years of work will pay off and he will be the first to see the structure of a protein no one has ever seen before.

Embedded in that pattern is the mathematical information needed to back-calculate to the position of the atoms in the protein, a process a bit like throwing a handful of pebbles in a lake and then calculating where they landed by the pattern of waves arriving at the shoreline.

Lee got the PMT from Haemonchus contortus to crystallize first, but there were technical issues with the diffraction pattern that would have made solving it technically and computationally very demanding.

"When the Plasmodium enzyme finally crystallized, Soon got four crystals kind of stacked on top of each other and each of them was paper thin," Jez says.

"I never thought it would work, but we took them to Argonne anyway and he actually did surgery under the microscope and cracked off a little tiny piece of it."

To everyone's surprise, he got a clean diffraction pattern from the crystal. "Because the Plasmodium enzyme was the smallest one and the easiest to work on, we pushed that one first," Jez says.

The moment of truth

"Once we had a Plasmodium crystal that was diffracting really well, we could try back-calculating to see whether we could extract the atom positions from the data," Jez says.

After the computer finished its calculations, Lee clicked a mouse button to see the results, which would reveal whether his years of work finally would pay off.

When Lee clicked the mouse, he got an electron density map in exceptionally sharp focus.

"When you see a map like that, it's like suddenly the wind has kicked up and you're sailing free," Jez says, "because there's this moment, like, before you click that button, no one has ever seen how this protein is put together in three dimensions. You're the first person to ever see it.

"The irony of it is we got such good quality diffraction pattern and electron density maps off such an ugly crystal," he says.

Lock and load

"Once you have the electron density map, the task is to build a structure that matches the amino acid sequence of the protein," Jez says.

"The first thing you do is put in the amino acid backbones and connect them together to form a chain. It's like having a long thread, each inch of which is an amino acid, and your job is to take that thread and move it in three dimensions through that electron density map."

The next step is to add the side chains that make one amino acid different from another, Jez says. "The amino acid sequence is known," he says. "Your goal is to match the way you string together the amino acids in the electron density map to that sequence."

"Once you have the overall structure, you can start to figure out how the enzyme works. The PMT enzyme is trying to join two molecules," Jez says. "To do that, it has to lock them in place so that the chemistry can happen, and then it has to let go of them.

"We think the protein has a lid that opens and closes," he says. "The active site stays open until the substrates enter, and then the lid clamps down, and when it clamps down it actually puts the substrates together."

Not only do infections by Plasmodium falciparum cause the most severe form of malaria, about 40 percent of the human population lives in areas where the parasite is endemic. Moreover, drugs that used to be effective against malaria are beginning to fail, in part because widespread drug counterfeiting has led to resistance.

New anti-malarial drugs are desperately needed, and the PMT protein is an ideal target. If PMT is disabled, the protozoan can't make cell membranes and it dies. Moreover, a drug that would kill Plasmodium might have minimal side effects on patients.

Although the process of identifying compounds that would target PMT is in the early stages, a handful of anti-parasitical compounds used to treat diseases are known to block PMT as well.

As for Lee, he has had a hard go of it, but now things are breaking his way. Plasmodium PMT is giving up its secrets, and the plant and nematode PMTs are coming along as well.

When he clicked the mouse button and a clean electron density map came up, he says, it was like seeing "the light at the end of a five-year-long tunnel."

Source: Washington University in St. Louis