Journal Article Hydroxyethyl cellulose matrix applied to serial crystallography

Sugahara, Michihiro  ,  Nakane, Takanori  ,  Masuda, Tetsuya  ,  Suzuki, Mamoru  ,  Inoue, Shigeyuki  ,  Song, Changyong  ,  Tanaka, Rie  ,  Nakatsu, Toru  ,  Mizohata, Eiichi  ,  Yumoto, Fumiaki  ,  Tono, Kensuke  ,  Joti, Yasumasa  ,  Kameshima, Takashi  ,  Hatsui, Takaki  ,  Yabashi, Makina  ,  Nureki, Osamu  ,  Numata, Keiji  ,  Nango, Eriko  ,  Iwata, So

72017-04-06 , Springer Nature
ISSN:2045-2322
Description
低ノイズ・低粘着性・低コストのタンパク質結晶輸送媒体を発見--生理条件に近いタンパク質の高分解能構造解析に期待--. 京都大学プレスリリース. 2017-04-20.
Serial femtosecond crystallography (SFX) allows structures of proteins to be determined at room temperature with minimal radiation damage. A highly viscous matrix acts as a crystal carrier for serial sample loading at a low flow rate that enables the determination of the structure, while requiring consumption of less than 1 mg of the sample. However, a reliable and versatile carrier matrix for a wide variety of protein samples is still elusive. Here we introduce a hydroxyethyl cellulose-matrix carrier, to determine the structure of three proteins. The de novo structure determination of proteinase K from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal of the praseodymium atom was demonstrated using 3, 000 diffraction images.
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http://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/220412/1/s41598-017-00761-0.pdf

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