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

Leidy A. Lammers, Bauke W. Dijkstra, Rob P. van Weeghel, Hendri H. Pas, George T. Robillard

Research output: Contribution to journalMeeting AbstractAcademic

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)310-312
Number of pages3
JournalJournal of Molecular Biology
Volume228
Issue number1
DOIs
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

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