Open AccessCrystallization and preliminary crystallographic analysis of the cellulose biosynthesis‐related protein CMCax from Acetobacter xylinum
Author(s) -
Kawano Shin,
Yasutake Yoshiaki,
Tajima Kenji,
Satoh Yasuharu,
Yao Min,
Tanaka Isao,
Munekata Masanobu
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910500206x
Subject(s) - crystallization , polyethylene glycol , crystallography , monomer , biosynthesis , cellulose , resolution (logic) , materials science , escherichia coli , acetobacter , chemistry , biochemistry , polymer , organic chemistry , gene , artificial intelligence , computer science , fermentation
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 P 6 1 or P 6 5 , with unit‐cell parameters a = b = 89.1, c = 94.2 Å. The predicted Matthews coefficient ( V M ) value is 3.0 Å 3 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 Å using synchrotron radiation.