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- 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
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- Tuesday, 04 April 2017
Membrane proteins perform critical functions in living cells related to signal transduction, transport and energy transformations, and, as such, are implicated in a multitude of malfunctions and diseases. However, a structural and functional understanding of membrane proteins is strongly lagging behind that of their soluble partners, mainly, due to difficulties associated with their solubilization and generation of diffraction quality crystals.
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- Thursday, 30 March 2017
The BioXFEL Center is proud to announce the recipients of the Postdoctoral Research Award, Benjamin Stauch and Ahmad Hosseinizadeh. Dr. Stauch is a Postdoctoral Research Associate in the group of Prof. Vadim Cherezov at the Bridge Institute of the University of Southern California in Los Angeles. He received his Master’s degree in Bioinformatics from the University of Frankfurt (Germany) in 2007 and carried out his doctoral research within the EMBL International Ph.D. Programme at EMBL Heidelberg (Germany) and the University of Cambridge (UK) where he obtained a Ph.D. in Biology in 2013.
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- Thursday, 30 March 2017
Serial femtosecond crystallography (SFX) takes advantage of extremely bright and ultrashort pulses produced by x-ray free-electron lasers (XFELs), allowing for the collection of high-resolution diffraction intensities from micrometer-sized crystals at room temperature with minimal radiation damage, using the principle of “diffraction-before-destruction.” However, de novo structure factor phase determination using XFELs has been difficult so far.
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- Friday, 24 March 2017
Arizona State University is currently seeking a research specialist. This position in experimental biophysics would assist scientists in collecting experimental data at the Linac Coherent Light Source (LCLS) X-ray laser near Stanford University, as part of the BioXFEL project https://www.bioxfel.org/.
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- Thursday, 16 March 2017
Describing the multiple conformations of proteins is important for understanding the relationship between molecular flexibility and function. However, most methods for interpreting data from X-ray crystallography focus on building a single structure of the protein, which limits the potential for biological insights. Here we introduce an improved algorithm for using crystallographic data to model these multiple conformations that addresses two previously overlooked types of protein backbone flexibility: peptide flips and glycine movements.
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- Tuesday, 14 March 2017
BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores.
More Articles...
- Structural enzymology using X-ray free electron lasers
- Coherent diffraction of single Rice Dwarf virus particles using hard X-rays at the Linac Coherent Light Source
- Three-dimensional-printed gas dynamic virtual nozzles for x-ray laser sample delivery
- XFEL data analysis for structural biology
- Structure solved from smallest protein crystals yet
