Abstract
The A-domain of the mannitol transport protein enzyme IImtl from Escherichia coli (relative molecular mass 16,300) was crystallized, both at room temperature and 4°C, from 40% polyethylene glycol 6000 (pH 8.5 to 9.0) using the hanging-drop method of vapour diffusion. The crystals have the monoclinic space group P21, with unit cell dimensions a = 54.0 Å, b = 67.0 Å, c = 80.9 Å and β = 100.8°. They diffract to 2.6 Å resolution. A self-rotation function and self-Patterson suggest that there are four molecules in the asymmetric unit showing mmm symmetry.
Original language | English |
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Pages (from-to) | 310-312 |
Number of pages | 3 |
Journal | Journal of Molecular Biology |
Volume | 228 |
Issue number | 1 |
DOIs | |
Publication status | Published - 5-Nov-1992 |
Keywords
- CRYSTALLIZATION
- MANNITOL TRANSPORT
- PHOSPHOTRANSFERASE
- ENZYME-II
- BACTERIAL PHOSPHOTRANSFERASE SYSTEM
- ESCHERICHIA-COLI
- ENZYME-IIIMTL
- PHOSPHOENOLPYRUVATE
- PERMEASE
- SEQUENCE
- PURIFICATION
- HOMOLOGY
- DETECTOR
- IIMTL