Purification, crystallization and preliminary X-ray studies of AxCesD required for efficient cellulose biosynthesis in Acetobacter xylinum.
AxCesD protein required for bacterial cellulose biosynthesis in Acetobacter xylinum was overexpressed in E. coli, purified and crystallized. Single crystals of SeMet-substituted AxCesD were obtained by the sitting-drop vapor-diffusion method. The crystal belongs to the primitive trigonal space group P3 2, with unit-cell parameters a = b = 77.7 A, and c = 213.9 A. The asymmetric unit in the crystal was assumed to contain 8 protein molecules giving the Matthews coefficient (VM) of 2.54 A3 Da(-1). Se-MAD data were collected to 2.3 A resolution using synchrotron radiations.
Hu
SongQing
S
Faculty of Advanced Life Science, Hokkaido University, 060-0810, Sapporo, Japan.
Gao
YongGui
Y
Tajima
Kenji
K
Yao
Min
M
Yoda
Takanori
T
Shimura
Daisuke
D
Satoh
Yasuharu
Y
Kawano
Shin
S
Tanaka
Isao
I
Munekata
Masanobu
M
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D002482:Cellulose / Q000096:biosynthesis*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D041822:Gluconacetobacter xylinus / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D002482:Cellulose