Crystallization of the hydantoin transporter Mhp1 from Microbacterium liquefaciens.
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.
Shimamura
Tatsuro
T
Human Receptor Crystallography Project, ERATO, Japan Science and Technology Agency, Yoshida-Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Yajima
Shunsuke
S
Suzuki
Shun'ichi
S
Rutherford
Nicholas G
NG
O'Reilly
John
J
Henderson
Peter J F
PJ
Iwata
So
S
D000192:Actinomycetales / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006827:Hydantoins / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D006827:Hydantoins; D008565:Membrane Proteins