| Literature DB >> 16511009 |
Shin Kawano1, Yoshiaki Yasutake, Kenji Tajima, Yasuharu Satoh, Min Yao, Isao Tanaka, Masanobu Munekata.
Abstract
The cellulose biosynthesis-related protein CMCax from Acetobacter xylinum was overexpressed in Escherichia coli, purified and crystallized. Single crystals of selenomethionine (SeMet) substituted CMCax were obtained by the hanging-drop vapour-diffusion method at 293 K, primarily using polyethylene glycol 4000 as a precipitant. The crystals belong to the primitive hexagonal space group P6(1) or P6(5), with unit-cell parameters a = b = 89.1, c = 94.2 A. The predicted Matthews coefficient (VM) value is 3.0 A3 Da(-1) for one CMCax monomer in the asymmetric unit. A single-wavelength anomalous dispersion (SAD) data set was collected to a resolution of 2.3 A using synchrotron radiation.Entities:
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Year: 2005 PMID: 16511009 PMCID: PMC1952249 DOI: 10.1107/S174430910500206X
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091