Crystallization and preliminary X-ray analysis of β-amylase from Bacillus polymyxa

Takashi Yamane, Hiroshi Tasaki, Fusako Matsumoto, Atsuo Suzuki, Nobuyuki Uozumi, Tamaichi Ashida

Research output: Contribution to journalArticlepeer-review

Abstract

A truncated β-amylase (E.C. 3.2.1.2) from Bacillus polymyxa has been crystallized using the hanging-drop vapour-diffusion method at 277 K. The crystals belong to the orthorhombic space group P212121 with cell dimensions a = 64.6, b = 141.9, c = 155.1 Å and diffract to 2.5 Å resolution. The asymmetric unit containing three protein molecules was derived from an electron-density map calculated at 4 Å resolution using MIR phases. This gives a V(m) value of 2.36 Å3 Da-1.

Original languageEnglish
Pages (from-to)898-900
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number4
DOIs
Publication statusPublished - 1999 Apr 1
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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