research papers
The combination of X-ray free-electron lasers (XFELs) with serial femtosecond crystallography represents cutting-edge technology in structural biology, allowing the study of enzyme reactions and dynamics in real time through the generation of `molecular movies'. This technology combines short and precise high-energy X-ray exposure to a stream of protein microcrystals. Here, the XFEL structure of carbonic anhydrase II, a ubiquitous enzyme responsible for the interconversion of CO2 and bicarbonate, is reported, and is compared with previously reported NMR and synchrotron X-ray and neutron single-crystal structures.
Keywords: carbonic anhydrase II; XFELs; X-ray crystallography; NMR; neutron diffraction crystallography; radiation damage.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S2059798324000482/lp5069sup1.pdf |
PDB references: human carbonic anhydrase II, room-temperature data set A, 8sd1; room-temperature data set B, 8sd6; room-temperature data set C, 8sd7; room-temperature data set D, 8sd8; room-temperature data set E, 8sd9; XFEL data set, 8sf1