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Crystal sample pins and a storage cassette system compatible with the protein crystallography beamlines at both the Photon Factory and SPring‐8
Author(s) -
Fujihashi Masahiro,
Hiraki Masahiko,
Ueno Go,
Baba Seiki,
Murakami Hironori,
Suzuki Mamoru,
Watanabe Nobuhisa,
Tanaka Isao,
Nakagawa Atsushi,
Wakatsuki Soichi,
Yamamoto Masaki,
Miki Kunio
Publication year - 2012
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s002188981203734x
Subject(s) - spring 8 , factory (object oriented programming) , spring (device) , synchrotron , crystal (programming language) , computer science , robot , synchrotron radiation , flexibility (engineering) , materials science , optics , protein crystallization , mechanical engineering , beam (structure) , physics , beamline , engineering , artificial intelligence , mathematics , statistics , crystallization , thermodynamics , programming language
Protein crystallography beamlines at the two major Japanese synchrotron facilities (SPring‐8 and Photon Factory) employ different crystal‐exchange robots. The robots SPACE and PAM, installed at SPring‐8 and the Photon Factory, respectively, accelerate crystal exchange and assist in the efficient use of beamtime. SPACE also supports customizable automatic data collection, in which an X‐ray beam is irradiated at a manually determined position during the crystal evaluation process. However, this data collection requires special crystal‐mounting screw pins made of polyacetal, which are not compatible with PAM. In order to give users the flexibility to collect diffraction data sets at either of the two synchrotrons, we have developed a compatible cassette system. Pins stored in the cassette can be mounted or demounted using either SPACE or PAM, and are compatible with the customizable automatic data collection provided by SPACE. Users can handle the pins and cassettes easily, employing common tools and techniques for efficient protein cryocrystallography experiments.