Atomic 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.
Atomic resolution structure of serine protease proteinase K at ambient temperature
T. Masuda,Mamoru Suzuki,S. Inoue,C. Song,T. Nakane,E. Nango,Rie Tanaka,K. Tono,Y. Joti,T. Kameshima,T. Hatsui,M. Yabashi,B. Mikami,O. Nureki,K. Numata,S. Iwata,M. Sugahara
Published 2017 in Scientific Reports
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- Publication year
2017
- Venue
Scientific Reports
- Publication date
2017-02-21
- Fields of study
Biology, Physics, Materials Science, Chemistry, Medicine
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Semantic Scholar, PubMed
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