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Crystallization of the A-Domain of the Mannitol Transport Protein Enzyme IImtl

Lammers, L. A., Dijkstra, B. W., Weeghel, R. P. V., Pas, H. H. & Robillard, G. T., 5-Nov-1992, In : Journal of Molecular Biology. 228, 1, p. 310-312 3 p.

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DOI

  • Leidy A. Lammers
  • Bauke W. Dijkstra
  • Rob P. van Weeghel
  • Hendri H. Pas
  • George T. Robillard
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 languageEnglish
Pages (from-to)310-312
Number of pages3
JournalJournal of Molecular Biology
Volume228
Issue number1
Publication statusPublished - 5-Nov-1992

    Keywords

  • CRYSTALLIZATION, MANNITOL TRANSPORT, PHOSPHOTRANSFERASE, ENZYME-II, BACTERIAL PHOSPHOTRANSFERASE SYSTEM, ESCHERICHIA-COLI, ENZYME-IIIMTL, PHOSPHOENOLPYRUVATE, PERMEASE, SEQUENCE, PURIFICATION, HOMOLOGY, DETECTOR, IIMTL

ID: 3325806