Crystallization and preliminary X-ray studies of Bacillus pumilus IPO xylanase

Hideaki Moriyama, Yasuo Hata, Hiroshi Yamaguchi, Mamoru Sato, Atsuhiko Shinmyo, Nobuo Tanaka, Hirosuke Okada, Yukiteru Katsube

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


The xylan-degrading enzyme xylanase, from Bacillus pumilus IPO, has been crystallized. The crystals are monoclinic, space group P21with a = 40.8 A ̊, b = 66.8 A ̊, c = 34.7 A ̊and β = 103.0 °. The asymmetric unit contains one molecule of Mr 22,500. The crystals diffract to at least 2.5 Å resolution, and they are suitable for X-ray crystal structure analysis at high resolution.

Original languageEnglish (US)
Pages (from-to)237-238
Number of pages2
JournalJournal of Molecular Biology
Issue number1
StatePublished - Jan 5 1987
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology


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