Popular Articles
- Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature
- NSF awards $22.5 million to capture biology at the atomic level using X-ray lasers
- BioXFEL Research Support Call for Proposals
- Frankuchen Award : ACA 2019
- UWM researchers create first 3D movie of virus in action
Archived Articles
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- Thursday, 08 June 2017
Cherezov lab members in association with researchers from The Scripps Research Institute, Moscow Institute of Physics and Technology, and Institute of Complex Systems have designed, synthesized, and characterized a series of chemically stable lipids resistant to hydrolysis capable of forming a lipidic cubic phase. The phase properties and lattice parameters of mesophases made of two most promising lipids were characterized. One of these lipids was used for crystallization and structure determination of a prototypical membrane protein bacteriorhodopsin at 4 and 20 °C.
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- Tuesday, 06 June 2017
Crystal structuredetermination of biological macromolecules using the novel technique of serial femtosecond crystallography (SFX) is severely limited by the scarcity of X-ray free-electron laser (XFEL) sources. However, recent and future upgrades render microfocus beamlines at synchrotron-radiation sources suitable for room-temperature serial crystallography data collection also.
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- Wednesday, 31 May 2017
X-ray crystallography at X-ray free-electron laser sources is a powerful method for studying macromolecules at biologically relevant temperatures. Moreover, when combined with complementary techniques like X-ray emission spectroscopy, both global structures and chemical properties of metalloenzymes can be obtained concurrently, providing insights into the interplay between the protein structure and dynamics and the chemistry at an active site.
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- Tuesday, 30 May 2017
Although protein design has been used to introduce new functions, designed variants generally only function as well as natural proteins after rounds of laboratory evolution. One possibility for this pattern is that designed mutants frequently sample nonfunctional conformations.
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- Tuesday, 23 May 2017
Burrowed deep under the foothills near Palo Alto, Calif., scientists scurried through an underground laboratory, making final preparations for a series of explosions. THEIR PLAN: blow up tiny crystals of proteins that could reveal one of nature's best-kept secrets—how plant photosynthesis turns light into chemical energy. The potential payoff: a step toward unlimited clean power.
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- Thursday, 18 May 2017
Nearly all protein functions require structural change, such as enzymes clamping onto substrates, and ion channels opening and closing. These motions are a target for possible new therapies; however, the control mechanisms are under debate. Calculations have indicated protein vibrations enable structural change. However, previous measurements found these vibrations only weakly depend on the functional state.
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- Diffraction data of core-shell nanoparticles from an X-ray free electron laser
- BioXFEL CoPI Appointed to DOE Advisory Committee
- Bacterial expression, correct membrane targeting and functional folding of the HIV-1 membrane protein Vpu using a periplasmic signal peptide
- BioXFEL collaborator Henry Chapman receives 2017 Roentgen Medal
- BioXFEL researchers uncover details of key drug target regulating blood pressure
