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 journalArticle

14 Scopus citations

Abstract

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
Volume193
Issue number1
DOIs
StatePublished - Jan 5 1987

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Crystallization and preliminary X-ray studies of Bacillus pumilus IPO xylanase'. Together they form a unique fingerprint.

  • Cite this

    Moriyama, H., Hata, Y., Yamaguchi, H., Sato, M., Shinmyo, A., Tanaka, N., Okada, H., & Katsube, Y. (1987). Crystallization and preliminary X-ray studies of Bacillus pumilus IPO xylanase. Journal of Molecular Biology, 193(1), 237-238. https://doi.org/10.1016/0022-2836(87)90644-9