Journal
SCIENTIFIC REPORTS
Volume 7, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/srep45604
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Funding
- Japan Synchrotron Radiation Research Institute (JASRI) [2015A8026, 2015A8048]
- BL26B1 of SPring-8 [2015A1052]
- X-ray FreeElectron Laser Priority Strategy Program (MEXT)
- Strategic Basic Research Program of Japan Science and Technology Agency (JST)
- Japan Society for the Promotion of Science [25650026]
- Platform for Drug Discovery, Informatics, and Structural Life Science (MEXT)
- NRF [2015R1A5A1009962, 2016R1A2B3010980]
- Grants-in-Aid for Scientific Research [26440028, 25650026] Funding Source: KAKEN
- National Research Foundation of Korea [2016R1A2B3010980] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Atomic resolution structures (beyond 1.20 angstrom) 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 angstrom 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.
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