Crystallization and preliminary crystallographic analysis of the cellulose biosynthesis-related protein CMCax from Acetobacter xylinum.
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.
Kawano
Shin
S
Division of Molecular Chemistry, Graduate School of Engineering, Hokkaido University, Kita-13, Nishi-8, Sapporo, Hokkaido 060-8628, Japan.
Yasutake
Yoshiaki
Y
Tajima
Kenji
K
Satoh
Yasuharu
Y
Yao
Min
M
Tanaka
Isao
I
Munekata
Masanobu
M
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D002482:Cellulose / Q000096:biosynthesis*; D003460:Crystallization; D041822:Gluconacetobacter xylinus / Q000737:chemistry / Q000378:metabolism*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D002482:Cellulose