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Crystallization of the hydantoin transporter Mhp1 from Microbacterium liquefaciens

DOI: 10.1107/S1744309108036920 DOI Help

Authors: Tatsuro Shimamura (Japan Science and Technology Agency) , Shunsuke Yajima (Imperial College London; Tokyo University of Agriculture) , Shun'ichi Suzuki (Aminosciences Laboratories; University of Leeds) , Nicholas G. Rutherford (University of Leeds) , John O'reilly (University of Leeds) , Peter J. F. Henderson (University of Leeds) , So Iwata (Japan Science and Technology Agency; Kyoto University; Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 64 (12) , PAGES 1172 - 1174

State: Published (Approved)
Published: December 2008

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 P212121, unit-cell parameters a = 79.7, b = 101.1, c = 113.8 Å). A complete data set has been collected from a single crystal to a resolution of 2.85 Å with 64 741 independent observations (94% complete) and an Rmerge of 0.12. Further experimental phasing methods are under way.

Journal Keywords: Transporters; Nucleobase:Cation Symporter 1 Family; Membrane Proteins; Hydantoins

Subject Areas: Biology and Bio-materials

Instruments: NONE-No attached Diamond beamline

Added On: 19/08/2009 23:07

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