- 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
- Room temperature structures beyond 1.5 Å by serial femtosecond crystallography
- Thursday, 19 March 2015 16:14
Determining the interconverting conformations of dynamic proteins in atomic detail is a major challenge for structural biology. Conformational heterogeneity in the active site of the dynamic enzyme cyclophilin A (CypA) has been previously linked to its catalytic function. Here we compare the conformational ensembles of CypA by fixed-target X-ray free electron laser (XFEL) crystallography and multitemperature synchrotron crystallography.