Open AccessApplication of a fine thread beam to the structure analysis of a hemihedrally twinned crystal of hydroxylamine oxidoreductase
Author(s) -
Igarashi Noriyuki,
Moriyama Hideaki,
Tanaka Nobuo
Publication year - 1998
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s0909049597017962
Subject(s) - crystal twinning , crystallography , crystal structure , hydroxylamine , materials science , diffraction , chemistry , physics , optics , microstructure , organic chemistry
Accurate diffraction intensity data have been collected from a twinned P 6 3 crystal of the 24‐haem protein hydroxylamine oxidoreductase, from a nitrifying chemoautotrophic bacterium Nitrosomonas europaea , using synchrotron radiation at station BL6A of the Photon Factory. Estimation of the twinning fraction and deconvoluted intensity data, including native and heavy‐atom derivative data, gave an improved Patterson function. Four diffraction data sets were collected from one crystal and an estimation of the twinning fraction to confirm the phenomena was undertaken. The successfully detwinned data sets were utilized in the structure analysis of the present enzyme. The mechanism of twinned‐crystal formation is also discussed.