News

UB receives $4.5 million from SUNY to recruit top faculty

UB has been awarded $4.5 million to hire world-class scholars whose work will boost the university’s research enterprise and educational offerings while enhancing innovation in the Buffalo Niagara region. The funding is comprised of three grants from SUNY’s Empire Innovation Program, which helps institutions recruit senior faculty members with track records of significant scholarly achievement and externally funded research projects.

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XFELs Open A New Era in Structural Chemical Biology

X-ray crystallography, the workhorse of structural biology, has been revolutionized by the advent of serial femtosecond crystallography using X-ray free electron lasers. Here, the fast pace and history of discoveries are discussed together with current challenges and the method's great potential to make new structural discoveries, such as the ability to generate molecular movies of biomolecules at work.

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Chemically Stable Lipids for Membrane Protein Crystallization

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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Serial millisecond crystallography of membrane

Crystal structure determination 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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Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers

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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Flexibility and Design: Conformational Heterogeneity along the Evolutionary Trajectory of a Redesigned Ubiquitin

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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