- Science Director Dr. John Spence named Royal Society Fellow
- BioXFEL Graduate Student Joey Olmos (Rice) Earns NSF Graduate Research Fellowship
- NSF BioXFEL researchers create a better way to find out ‘when’
- Mapping Conformational Landscape Through Crystallography
- Taking the initiative on single particle imaging
- Tuesday, 11 July 2017 11:53
Bacteria live in complex ecologies, filled with competitors, environmental dangers, and defensive hosts. They face these challenges in many ways: by gathering together into tough biofilm communities, by sharing genetic information encoding useful proteins, and by picking up and moving when things look better elsewhere.
- Friday, 07 July 2017 11:01
The central hub for powerful electron beams at the Department of Energy’s SLAC National Accelerator Laboratory is getting a makeover to prepare for the installation of LCLS-II – a major upgrade to the Linac Coherent Light Source (LCLS), the world’s first hard X-ray free-electron laser. LCLS-II will deliver the most powerful X-rays ever made in a lab, with beams that are 10,000 times brighter than before, opening up unprecedented research opportunities in chemistry, materials science, biology and energy research.
- Thursday, 06 July 2017 14:04
World's largest X-ray laser starts operation - milestone en route to official opening on September 1. The world’s largest X-ray laser, the European XFEL, has entered its operation phase, a press release said Tuesday (July 4, 2017). The X-ray laser produces extremely bright and short X-ray flashes with the help of specialised experiment stations and gives scientists entirely new insights into the atomic details and processes of the nano world.
- Wednesday, 05 July 2017 12:12
Riboswitches are structurally dynamic RNA molecules, undergoing changes in shape as they perform their regulatory functions. Riboswitches typically have two domains: a ligand-binding “aptamer” domain that changes conformation when it binds to a specific ligand, which then sends a signal to an “expression platform” domain that regulates use of the RNA.
- Thursday, 29 June 2017 13:11
Serial femtosecond X-ray crystallography (SFX) using an X-ray free electron laser (XFEL) is a recent advancement in structural biology for solving crystal structures of challenging membrane proteins, including G-protein coupled receptors (GPCRs), which often only produce microcrystals. An XFEL delivers highly intense X-ray pulses of femtosecond duration short enough to enable the collection of single diffraction images before significant radiation damage to crystals sets in.
- Tuesday, 27 June 2017 13:30
BioXFEL researchers in collaboration with others established a procedure for serial femtosecond crystallography (SFX) in lipidic cubic phase (LCP) for protein structure determination at X-ray free-electron lasers (XFELs). LCP-SFX uses the gel-like LCP as a matrix for growth and delivery of membrane protein microcrystals for crystallographic data collection.
- UB receives $4.5 million from SUNY to recruit top faculty
- XFELs Open A New Era in Structural Chemical Biology
- Chemically Stable Lipids for Membrane Protein Crystallization
- Serial millisecond crystallography of membrane
- Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers