Atomic resolution structure of serine protease proteinase K at ambient temperature
SCIE
SCOPUS
- Title
- Atomic resolution structure of serine protease proteinase K at ambient temperature
- Authors
- Masuda, T.; Suzuki, M.; Inoue, S.; Song, C.; Nakane, T.; Nango, E.; Tanaka, R.; Tono, K.; Joti, Y.; Kameshima, T.; Hatsui, T.; Yabashi, M.; Mikami, B.; Nureki, O.; Numata, K.; Iwata, S.; Sugahara, M.
- Date Issued
- 2017-03
- Publisher
- Nature Publishing Group
- Abstract
- Atomic resolution structures (beyond 1.20 ?) 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 ? 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. ? 2017 The Author(s).
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/92124
- DOI
- 10.1038/srep45604
- ISSN
- 2045-2322
- Article Type
- Article
- Citation
- Scientific Reports, vol. 7, 2017-03
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