Hydroxyethyl cellulose matrix applied to serial crystallography View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

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

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. More... »

PAGES

703

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41598-017-00761-0

    DOI

    http://dx.doi.org/10.1038/s41598-017-00761-0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1084130857

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/28386083


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