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 language | English |
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Pages (from-to) | 1212-1214 |
Number of pages | 3 |
Journal | Acta Crystallographica. Section D, Biological Crystallography |
Volume | 55 |
Publication status | Published - Jun 1999 |
Keywords
- SUGAR PHOSPHOTRANSFERASE SYSTEM
- GRAM-POSITIVE BACTERIA
- ESCHERICHIA-COLI K12
- FUSOBACTERIUM-MORTIFERUM
- FAMILY 4
- PHOSPHOENOLPYRUVATE
- PROTEINS
- SEQUENCE
- CLASSIFICATION
- EXPRESSION