Crystallization and preliminary X-ray analysis of beta-glucan exohydrolase isoenzyme ExoI from barley (Hordeum vulgare).
Crystals of a beta-glucan exohydrolase purified from extracts of young barley seedlings have been obtained by vapour diffusion in the presence of ammonium sulfate and polyethylene glycol. The enzyme exhibits broad substrate specificity against (1,3)-, (1,3;1,4)- and (1,3;1,6)-beta-glucans, and related oligosaccharides. Crystal dimensions of up to 0.8 x 0.4 x 0.6 mm have been observed. The crystals belong to the tetragonal space group P41212 or P43212. Cell parameters are a = b = 102.1 and c = 184.5 A, and there appear to be eight molecules in the asymmetric unit. The crystals diffract to at least 2.2 A resolution using X-rays from a rotating-anode generator.
Hrmova
M
M
Department of Plant Science, University of Adelaide, Waite Campus, SA 5064, Australia.
Varghese
J N
JN
Høj
P B
PB
Fincher
G B
GB
D003460:Crystallization; D018360:Crystallography, X-Ray; D043326:Glucan 1,3-beta-Glucosidase; D001467:Hordeum / Q000201:enzymology*; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D001617:beta-Glucosidase / Q000737:chemistry* / Q000302:isolation & purification
D007527:Isoenzymes; D010940:Plant Proteins; D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase