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

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JournalActa Crystallographica Section D: Biological Crystallography
DatePublished - Jun 1999
Volume55
Number of pages3
Pages (from-to)1212-1214
Original languageEnglish

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.

    Research areas

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

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