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Neutron photographic measurements of protein single‐crystal reflections
Author(s) -
Hohlwein D.,
Mason S. A.
Publication year - 1981
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/s0021889881008601
Subject(s) - microdensitometer , diffractometer , optics , neutron , protein crystallization , crystal (programming language) , triclinic crystal system , resolution (logic) , materials science , neutron diffraction , chemistry , physics , crystallography , diffraction , crystal structure , nuclear physics , computer science , scanning electron microscope , crystallization , artificial intelligence , programming language , organic chemistry
Photographic neutron intensity measurements on a 2 mm 3 single‐crystal of triclinic lysozyme are compared with conventional neutron diffractometer data. The reflections were recorded with the oscillation technique. The structure factors were derived from the optical densities scanned by an automatic microdensitometer and processed by computer programs. A statistical analysis shows that the photographic data are of about the same accuracy as recently collected diffractometer data. For the same flux and crystal volume the data collection time is reduced by up to two orders of magnitude.