- ASU Hosts Nozzle Maker Workshop
- XFEL Science Highlighted in Nature
- BioXFEL researchers capture the highest-resolution protein snapshots ever taken with an X-ray laser, revealing new details in a well-studied protein that acts as an “eye” in bacteria.
- Science Director Dr. John Spence named Royal Society Fellow
- BioXFEL Graduate Student Joey Olmos (Rice) Earns NSF Graduate Research Fellowship
Bacterial expression, correct membrane targeting and functional folding of the HIV-1 membrane protein Vpu using a periplasmic signal peptide
- Thursday, 20 April 2017 11:17
Structural analysis of membrane proteins has traditionally been bottlenecked by the lack of sufficiently large amounts of pure, properly folded and functional membrane proteins. The issue is particularly important considering the fact that membrane proteins constitute a significant proportion of clinical drug targets.
- Tuesday, 11 April 2017 13:13
DESY scientist Henry Chapman has been awarded the Roentgen Medal by the city of Remscheid. The town in which Wilhelm Conrad Roentgen was born has been presenting this award annually since 1951 to individuals who have made outstanding contributions towards improving and advancing the use of the radiation discovered by Roentgen. Henry Chapman, a Leading Scientist at DESY and professor at the University of Hamburg, has been awarded the Medal in recognition of his pioneering work on the application of X-ray lasers for determining the structure of biological macromolecules.
- Tuesday, 11 April 2017 09:53
Designing molecules that selectively bind to a specific receptor type is often challenging, but can be crucial for different therapeutic purposes. Both angiotensin II receptors are important drug targets, since the blockade of AT 1 R has anti-hypertensive effects, while the modulation of AT 2 R could be useful for cardioprotection, neuropathic pain relief and the treatment of several other conditions.
The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography
- Thursday, 06 April 2017 09:14
Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the room temperature crystal structure of the chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 Å resolution.
- Tuesday, 04 April 2017 13:11
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.
- Thursday, 30 March 2017 12:58
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.
- Native phasing of x-ray free-electron laser data for a G protein–coupled receptor
- Job Opening: Research Specialist
- Exposing Hidden Alternative Backbone Conformations in X-ray Crystallography Using qFit
- De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure
- Structural enzymology using X-ray free electron lasers