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Hydroxyethyl cellulose matrix applied to serial crystallography.

ABSTRACT: 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.

SUBMITTER: Sugahara M

PROVIDER: S-EPMC5429652 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

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Hydroxyethyl cellulose matrix applied to serial crystallography.

Sugahara Michihiro M Nakane Takanori T Masuda Tetsuya T Suzuki Mamoru M Inoue Shigeyuki S Song Changyong C Tanaka Rie R Nakatsu Toru T Mizohata Eiichi E Yumoto Fumiaki F Tono Kensuke K Joti Yasumasa Y Kameshima Takashi T Hatsui Takaki T Yabashi Makina M Nureki Osamu O Numata Keiji K Nango Eriko E Iwata So S

Scientific reports 20170406 1

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 c ...[more]

PMID: 28386083

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