Author:
Masuda Tetsuya,Suzuki Mamoru,Inoue Shigeyuki,Song Changyong,Nakane Takanori,Nango Eriko,Tanaka Rie,Tono Kensuke,Joti Yasumasa,Kameshima Takashi,Hatsui Takaki,Yabashi Makina,Mikami Bunzo,Nureki Osamu,Numata Keiji,Iwata So,Sugahara Michihiro
Abstract
AbstractAtomic resolution structures (beyond 1.20 Å) at ambient temperature, which is usually hampered by the radiation damage in synchrotron X-ray crystallography (SRX), will add to our understanding of the structure-function relationships of enzymes. Serial femtosecond crystallography (SFX) has attracted surging interest by providing a route to bypass such challenges. Yet the progress on atomic resolution analysis with SFX has been rather slow. In this report, we describe the 1.20 Å resolution structure of proteinase K using 13 keV photon energy. Hydrogen atoms, water molecules, and a number of alternative side-chain conformations have been resolved. The increase in the value of B-factor in SFX suggests that the residues and water molecules adjacent to active sites were flexible and exhibited dynamic motions at specific substrate-recognition sites.
Publisher
Cold Spring Harbor Laboratory