Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution x-ray diffraction.
Acetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals diffract to better than 1 A resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P2(1)2(1)2(1) and cell dimensions are a = 34.9 A, b = 61.0 A, C = 72.5 A.
Pangborn
W
W
Hauptman-Woodward Medical Research Institute, Inc., Buffalo, New York 14203, USA.
Erman
M
M
Li
N
N
Burkhart
B M
BM
Pletnev
V Z
VZ
Duax
W L
WL
Gutierrez
R
R
Peirano
A
A
Eyzaguirre
J
J
Thiel
D J
DJ
Ghosh
D
D
D000115:Acetylesterase / Q000737:chemistry*; D010407:Penicillium / Q000201:enzymology*; D014961:X-Ray Diffraction
D000115:Acetylesterase; C081851:acetylxylan esterase