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

Noriyuki Igarashi, Hideaki Moriyama, Nobuo Tanaka

Research output: Contribution to journalArticle

Abstract

Accurate diffraction intensity data have been collected from a twinned P63 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.

Original languageEnglish (US)
Pages (from-to)975-976
Number of pages2
JournalJournal of Synchrotron Radiation
Volume5
Issue number3
DOIs
StatePublished - May 1 1998

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threads
Twinning
twinning
Crystals
Diffraction
crystals
Synchrotron radiation
industrial plants
diffraction
bacteria
Industrial plants
enzymes
Bacteria
synchrotron radiation
Photons
Enzymes
stations
Derivatives
proteins
Proteins

Keywords

  • Haems
  • Hydroxylamine oxidoreductase
  • Structures

ASJC Scopus subject areas

  • Radiation
  • Nuclear and High Energy Physics
  • Instrumentation

Cite this

Application of a fine thread beam to the structure analysis of a hemihedrally twinned crystal of hydroxylamine oxidoreductase. / Igarashi, Noriyuki; Moriyama, Hideaki; Tanaka, Nobuo.

In: Journal of Synchrotron Radiation, Vol. 5, No. 3, 01.05.1998, p. 975-976.

Research output: Contribution to journalArticle

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