Crystallization of the hydantoin transporter Mhp1 from Microbacterium liquefaciens

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Dec 1;64(Pt 12):1172-4. doi: 10.1107/S1744309108036920. Epub 2008 Nov 28.

Abstract

The integral membrane protein Mhp1 from Microbacterium liquefaciens transports hydantoins and belongs to the nucleobase:cation symporter 1 family. Mhp1 was successfully purified and crystallized. Initial crystals were obtained using the hanging-drop vapour-diffusion method but diffracted poorly. Optimization of the crystallization conditions resulted in the generation of orthorhombic crystals (space group P2(1)2(1)2(1), unit-cell parameters a = 79.7, b = 101.1, c = 113.8 A). A complete data set has been collected from a single crystal to a resolution of 2.85 A with 64 741 independent observations (94% complete) and an R(merge) of 0.12. Further experimental phasing methods are under way.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinomycetales / metabolism*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Hydantoins / metabolism*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism

Substances

  • Bacterial Proteins
  • Hydantoins
  • Membrane Proteins