Journal Article Atomic resolution structure of serine protease proteinase K at ambient temperature.

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

72017-03-31 , Springer Nature
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.
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.

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