Crystallization and preliminary X-ray analysis of the 6-phospho-alpha-glucosidase from Bacillus subtilis

A Varrot, H Yamamoto, J Sekiguchi, J Thompson, G J Davies

Research output: Contribution to journalArticlepeer-review

Abstract

6-Phospho-alpha-glucosidase (GIvA) is the protein involved in the dissimilation of a-glycosides accumulated viaaphosphoenolpyruvate-dependent maltose phosphotransferase system (PEP-PTS) in Bacillus subtilis. The purified enzyme has been crystallized in a form suitable for X-ray diffraction analysis. Thin rod-like crystals have been grown by the hanging-drop method in the presence of manganese and NAD. They diffract beyond 22 Angstrom using synchrotron radiation and belong to the space group I222 (or its enantiomorph) with unit-cell dimensions a = 83.26, b = 102.56, c = 145.31 Angstrom and contain a single molecule of GIvA in the asymmetric unit.

Original languageEnglish
Pages (from-to)1212-1214
Number of pages3
JournalActa Crystallographica. Section D, Biological Crystallography
Volume55
Publication statusPublished - Jun 1999

Keywords

  • SUGAR PHOSPHOTRANSFERASE SYSTEM
  • GRAM-POSITIVE BACTERIA
  • ESCHERICHIA-COLI K12
  • FUSOBACTERIUM-MORTIFERUM
  • FAMILY 4
  • PHOSPHOENOLPYRUVATE
  • PROTEINS
  • SEQUENCE
  • CLASSIFICATION
  • EXPRESSION

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