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Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography

Nature Structural Biology volume 4, pages 909–914 (1997)Cite this article

Abstract

Neutron quasi-Laue diffraction data (2 Å resolution) from tetragonal hen egg-white lysozyme were collected in ten days with neutron imaging plates. The data processing Laue software, LAUEGEN, developed for X-ray Laue diffractometry, was adapted for neutron diffractometry with a cylindrical detector. The data analysis software, X-PLOR, was modified and used for the refinement of hydrogen atoms, and the positions of 960 hydrogen atoms in the protein and 157 bound water molecules, were determined. Several examples are given of the methods used to identify hydrogen atoms and water molecules.

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Authors and Affiliations

  1. Advanced Science Research Center, Japan Atomic Energy Research Institute, Ibaraki-ken, Naka-gun, Tokai-mura, 319-11, Japan

    Nobuo Niimura & Yoshiaki Minezaki

  2. Department of BioEngineering, Nagaoka University of Technology, Kamitomioka, Nagaoka, Niigata, Japan

    Takamasa Nonaka

  3. EMBL Outstation, Avenue des Martyrs, F38042, Grenoble, France

    Jean-Charles Castagna, Florent Cipriani & Clive Wilkinson

  4. ILL, Avenue des Martyrs, F38042, Grenoble, France

    Peter Høghøj & Mogens S. Lehmann

  5. On leave from Tohoku University,

    Nobuo Niimura

Authors
  1. Nobuo Niimura
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  2. Yoshiaki Minezaki
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  3. Takamasa Nonaka
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  4. Jean-Charles Castagna
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Correspondence to Nobuo Niimura.

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Niimura, N., Minezaki, Y., Nonaka, T. et al. Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography. Nat Struct Mol Biol 4, 909–914 (1997). https://doi.org/10.1038/nsb1197-909

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