Crystallization and preliminary crystallographic analysis of beta-L-arabinopyranosidase from Streptomyces avermitilis NBRC14893.
Beta-L-arabinopyranosidase from Streptomyces avermitilis NBRC14893 is a monomeric protein consisting of a catalytic domain belonging to glycosyl hydrolase family 27, an unknown domain and a substrate-binding domain belonging to carbohydrate-binding module family 13. The complete enzyme (residues 45-658) has successfully been cloned and homologously expressed in the Streptomyces expression system. beta-L-Arabinopyranosidase was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to 1.6 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.2, b = 98.9, c = 181.3 A. The Matthews coefficient was calculated to be 2.38 A(3) Da(-1).
Fujimoto
Zui
Z
Protein Research Unit, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan.
Ichinose
Hitomi
H
Harazono
Koichi
K
Honda
Mariko
M
Uzura
Atsuko
A
Kaneko
Satoshi
S
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D003625:Data Collection; D005798:Genes, Bacterial; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D010957:Plasmids; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D013223:Statistics as Topic; D013302:Streptomyces / Q000201:enzymology*; D017356:Synchrotrons; D014169:Transformation, Bacterial; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; C074451:Endo-arabinase; D006026:Glycoside Hydrolases