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.


Mapping the Conformational Landscape of a Dynamic Enzyme by XFEL and Multitemperature Crystallography