Application of a fine thread beam to the structure analysis of a hemihedrally twinned crystal of hydroxylamine oxidoreductase

Accurate diffraction intensity data have been collected from a twinned P6(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...

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Veröffentlicht in:Journal of synchrotron radiation. - 1994. - 5(1998), Pt 3 vom: 01. Mai, Seite 975-6
1. Verfasser: Igarashi, N (VerfasserIn)
Weitere Verfasser: Moriyama, H, Tanaka, N
Format: Aufsatz
Sprache:English
Veröffentlicht: 1998
Zugriff auf das übergeordnete Werk:Journal of synchrotron radiation
Schlagworte:Journal Article
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245 1 0 |a Application of a fine thread beam to the structure analysis of a hemihedrally twinned crystal of hydroxylamine oxidoreductase 
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520 |a Accurate diffraction intensity data have been collected from a twinned P6(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 
650 4 |a Journal Article 
700 1 |a Moriyama, H  |e verfasserin  |4 aut 
700 1 |a Tanaka, N  |e verfasserin  |4 aut 
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