Articles tagged with Protein Crystals
Two researchers from the Technical University of Munich have won an International Space Station Research Competition to study the structure of Hepatitis C virus proteins in microgravity. The project aims to identify new targets for medications and could lead to breakthroughs in treating the disease, which is prevalent in Egypt.
Scientists from Aalto University create ordered structures by mixing oppositely charged proteins and virus particles, enabling modular functionalization with various ligands. The method opens possibilities for biomedical and materials science research.
Researchers at HZB's BESSY II have discovered a new class of materials using protein crystalline frameworks, which can achieve high stability and be intricately interconnected. The discovery allows for controllable interpenetration and variability, opening up potential applications.
Scientists have developed a method to study protein crystals inside cells using X-ray analysis, bypassing complex sample preparation. This breakthrough enables the analysis of micron-scale in vivo samples with improved signal-to-noise ratio.
University of Missouri researchers have completed a 3D map of the Proline utilization A (PutA) enzyme, which facilitates metabolism by adding oxygen to molecules. This understanding will help drug manufacturers create more effective treatments for diseases like h. pylori infection.
A team at Washington University in St. Louis solved the structure of NolR, a master off-switch for the nodulation process that converts bacteria into nitrogen-fixing organisms. The discovery provides insight into the biological machinery of nitrogen-fixing and may lead to re-engineering crop plants with on-site nitrogen-fixing systems.
Researchers have successfully imaged a single layer of proteins using exceptionally bright and fast X-rays, significantly broadening the number and type of proteins that can be studied. This new method, based on XFEL technology, opens up possibilities for understanding protein structures and their role in disease and toxicity.
Researchers used computer simulation to analyze X-ray crystallographic data and found that current software programs underestimate the level of dynamics in proteins. This could lead to more accurate pictures of protein structures and improved development of medicines.
A team of scientists has discovered the structure of the NS1 protein, which helps dengue and West Nile viruses replicate and evade the immune system. The researchers believe this breakthrough could lead to the development of a vaccine that protects people without increasing their risk.
Researchers from Argonne National Laboratory and the University of Washington have identified a method to minimize radiation damage in protein crystals using submicrometer line focusing. This technique enables scientists to collect better data while reducing time and cost associated with repeated experiments.
Researcher Peter Vekilov will test his theories on crystal formation in space, studying how liquids transform into crystals. His work could lead to more efficient large-scale production methods.
Researchers used an X-ray free-electron laser to determine the structure of trypanosomal Cathepsin B, a promising target for treating sleeping sickness. The study provides detailed insight into how the naturally occurring native inhibitor binds, offering new ideas for designing targeted treatments.
Researchers at SLAC National Accelerator Laboratory have identified a new way to attack Helicobacter pylori, a bacterium that causes ulcers and stomach cancer. By pinpointing the Achilles' heel of this tough bacteria, scientists hope to develop specific and effective treatments.
Researchers at Ruhr-University Bochum developed a new method for studying the interaction between pharmaceuticals and their target proteins. The new technique uses infrared difference spectroscopy, which allows for the analysis of dynamic processes in proteins that were previously inaccessible.
Researchers at Leiden University have crystallized the adenosine A2A receptor to a record-breaking high resolution, allowing for detailed study of its structure and function. This breakthrough provides new insights into the mechanisms underlying Parkinson's disease and the effects of caffeine.
University of Pennsylvania chemists developed a theoretical method and computer algorithm to search for proteins that can crystallize into a target structure. They successfully created the first custom-designed protein crystal, paving the way for better understanding of proteins' makeup and designing new materials.
The study found that far fewer images are needed to map a protein's structure than previously believed, allowing for faster and more efficient imaging. The team also created a three-dimensional model of the protein using just 265 images.
Researchers at Washington University in St. Louis have identified seven genes encoding mechanosensitive channels in Arabidopsis thaliana, a small flowering plant related to mustard and cabbage. These channels are believed to play a crucial role in plant movement and response to physical stimuli.
Researchers have deciphered the structure of an essential enzyme in photosynthetic organisms, a target for algaecide development. This discovery could lead to the creation of compounds that block the enzyme's function, inhibiting algae growth without harming other plant life.
Scientists at Imperial College London have developed a new method to make proteins form crystals using 'smart materials' that remember the shape and characteristics of the molecule. This technique should assist research into new medicines by helping scientists work out the structure of drug targets.
Antifreeze proteins have been found to bind to ice crystals through a specific mechanism involving hydrophobic and hydrophilic groups. This discovery may lead to the development of stronger, more versatile AFPs with commercial applications in various industries.
Researchers have discovered a Bt protein that is highly effective at curing intestinal parasitic roundworm infections in humans. The Cry5B protein produced by the Bt bacterium is three times better than tribendimidine and shows promise as an alternative to existing treatments.
The Compact Light Source has achieved three key milestones: first scientific publication, micro-tomographic images, and protein crystallography data set. These results demonstrate its potential to transform biomedical research with high-intensity, tunable x-ray beams.
Scientists discover enzyme crucial for methanogenesis, a process releasing methane and carbon dioxide into the atmosphere. The findings could improve industrial processes and provide insights into natural biology's impact on climate change.
Using a bioinspired approach, researchers mimicked magnetotactic bacteria to synthesize ferromagnetic nanoparticles with desirable magnetic properties. The team successfully produced cobalt-ferrite nanoparticles, which have more desirable magnetic properties than magnetite.
Scientists at Northwestern University are mapping parts of lethal bacteria in three dimensions, exposing a fresh opening into the bacteria's vulnerabilities. This view will enable scientists to create drugs to disable or vaccines to prevent deadly infectious diseases such as anthrax, plague, and Ebola.
Researchers have performed the first atomic-detail computer simulation of how proteins vibrate in a crystal, enabling testing with new neutron analysis tools. The study aims to understand protein-protein interactions and could lead to breakthroughs in understanding biological systems.
Andrzej Joachimiak and Gerold Rosenbaum receive the award for their key contributions to protein crystallography research at Argonne National Laboratory. The recognition highlights the quality of their work in structural genomics and biophysics.
The Protein Structure Initiative (PSI) has established a materials repository and knowledgebase to share resources with the scientific community. The PSI-Materials Repository will store and ship clones of proteins, while the Knowledgebase will provide access to structural information and experimental details.
Scientists have discovered a natural protein produced by Bacillus thuringiensis that is highly effective at treating hookworm infections and curing anemia. The protein, called Cry5B, targets both developing and adult parasites, and can be produced inexpensively and safely for humans.
Researchers at Duke University Medical Center discovered a subtle 'backrub' motion in proteins, which could have important implications for understanding protein evolution and design. The study found that this motion is common in proteins frozen in crystals and may be even more prevalent in liquid environments.
Researchers at Imperial College London have made a significant breakthrough in protein crystal formation using a novel porous material called BioGlass. The team successfully induced the crystallization of the largest number of proteins ever achieved using a single nucleant, offering new hope for drug discovery.
Scientists have discovered how a biomolecule can act as a light switch, revealing its potential for high-resolution microscopy and optical data storage. The protein, asFP595, switches between fluorescent and non-fluorescent states using a tiny molecular mechanism.
Scientists have developed a new method for crystallizing proteins, which could lead to the creation of effective drugs for diseases such as cystic fibrosis and Alzheimer's. The improved method uses a thinner sponge-like structure to bind proteins together more easily.
A team from PNNL and USC has identified the region of a protein that interacts with crystals to form enamel, a material with entirely different properties from bone. The discovery explains how proteins can control crystal structure, enabling nano-patterning and nano-building.
A new 'hyperactive' antifreeze protein has been identified in the blood of winter flounder, enabling them to withstand temperatures as low as -1.9 degrees Celsius. This discovery explains the previously unknown mechanism behind these fish's survival in polar oceans.
Scientists use 'targeted mutagenesis' to make proteins more amenable to crystallization, shedding light on the plague and other diseases. The technique has already solved the structures of stubborn proteins like V antigen of Yersinia pestis.
Elves automates X-ray crystallography process, decreasing time to 19 minutes from days or weeks, increasing efficiency of beamlines. The software uses X-ray diffraction data to produce a 3-D layout of proteins, crucial for understanding their function and designing drugs.
A new technique developed by UCSD researcher Virgil Woods employs DXMS to identify unstructured regions in proteins that interfere with crystallization. Removing these regions through 'molecular surgery' enables proteins to crystallize well, overcoming a major obstacle in structural genomics.
Researchers at UH have discovered why insulin crystals do not form a certain defect called step bunching, which can lead to defects in crystals used in lasers. Understanding this process can help improve crystal-growing methods and lead to breakthroughs in medicine and technology.
Researchers at Purdue University have successfully crystallized a fat-soluble protein using a synthetic detergent and synthetic fat, overcoming a 20-year hurdle. This breakthrough could lead to significant advances in understanding diseases by studying the structure of these proteins.
Researchers have discovered that Bt toxins can kill a range of parasitic nematode species, including those affecting humans, animals, and crops. The findings suggest the potential for developing an inexpensive and environmentally safe means of controlling parasitic roundworms.
Researchers have determined the structure of the HER3 receptor, providing a blueprint for designing new drugs that target this protein. The discovery has significant implications for cancer treatment, particularly for breast cancer patients who may benefit from alternative strategies to Herceptin.
The American Cancer Society has awarded a $768,000 grant to Dr. Gloria Borgstahl to study the molecular processes that cause breast cancer. She is conducting related experiments on the International Space Station to understand how good cells turn bad and develop new treatments for the disease.
Scientists at the University of Illinois developed a lensless X-ray microscope that can image microscopic crystals in three dimensions. This technique offers potential for studying nanocrystalline materials and protein crystals, providing new insights into their growth mechanisms.
Scientists observed stress-driven reordering of a distorted protein crystal without thermal activation at low temperatures. The reordering was driven by mass transport caused by radiation damage, resulting in the formation of order in the system.
Bacteriorhodopsin, a salt-loving organism's defense mechanism, is grown in space to produce stable crystals, offering new insights into complex membrane proteins and their applications in all-optical computing. The findings may lead to the development of battery-conserving computer displays.
Researchers from NASA and French-American teams crystallized thaumatin in space, producing larger and more defect-free crystals with improved x-ray diffraction properties. This breakthrough paves the way for better understanding of the molecule's shape and function, potentially leading to new treatments for diabetes and obesity.
Researchers at the University of Chicago have discovered a new protein, calgranulin, that can prevent the formation of kidney stones in minute amounts. Calgranulin is present in the kidney and human urine and can stop the growth of calcium oxalate crystals, the major component of kidney stones.
The STS-89 mission will conduct experiments on granular materials, studying their behavior under conditions that cannot be simulated on Earth. The Mechanics of Granular Materials experiment will make twice as many test runs under an expanded range of conditions, potentially leading to great ramifications for down-to-Earth engineering. ...
Scientists are using NASA's Michelson interferometer to study protein crystal growth in space, a method that may lead to new treatments for diseases. The device, which was originally used to test the existence of the luminiferous ether, is being repurposed to analyze how molecules assemble into crystals.