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. © International Union of Crystallography 2008.
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Shimamura, T., Yajima, S., Suzuki, S., Rutherford, N. G., O’Reilly, J., Henderson, P. J. F., & Iwata, S. (2008). Crystallization of the hydantoin transporter Mhp1 from Microbacterium liquefaciens. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(12), 1172–1174. https://doi.org/10.1107/S1744309108036920
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