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Title: Atomic resolution structure of serine protease proteinase K at ambient temperature.
Authors: Masuda, Tetsuya  kyouindb  KAKEN_id  orcid (unconfirmed)
Suzuki, Mamoru
Inoue, Shigeyuki
Song, Changyong
Nakane, Takanori
Nango, Eriko  kyouindb  KAKEN_id
Tanaka, Rie
Tono, Kensuke
Joti, Yasumasa
Kameshima, Takashi
Hatsui, Takaki
Yabashi, Makina
Mikami, Bunzo  kyouindb  KAKEN_id
Nureki, Osamu
Numata, Keiji
Iwata, So  kyouindb  KAKEN_id
Sugahara, Michihiro
Author's alias: 桝田, 哲哉
鈴木, 守
岩田, 想
菅原, 道泰
Issue Date: 31-Mar-2017
Publisher: Springer Nature
Journal title: Scientific reports
Volume: 7
Thesis number: 45604
Abstract: 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.
Description: 酵素の立体構造、「SACLA」のX線レーザーを用いて常温、原子分解能構造解析に成功--体内に近い環境での酵素反応機構解明から、新薬や機能性分子創生に期待--. 京都大学プレスリリース. 2017-04-07.
Rights: © The Author(s) 2017. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit
DOI(Published Version): 10.1038/srep45604
PubMed ID: 28361898
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