Crystallization and preliminary diffraction analysis of a beta-galactosidase from Trichoderma reesei.
An extracellular beta-galactosidase from Trichoderma reesei was crystallized from sodium cacodylate buffer using polyethylene glycol (PEG) as a precipant. Crystals grown by homogenous streak-seeding belonged to space group P1, with unit-cell parameters a = 67.3, b = 69.1, c = 81.5 A, alpha = 109.1, beta = 97.3, gamma = 114.5 degrees . The crystals diffracted to 1.8 A resolution using a rotating-anode generator and to 1.2 A resolution using a synchrotron source. On the basis of the Matthews coefficient (V(M) = 3.16 A(3) Da(-1)), one molecule is estimated to be present in the asymmetric unit. The aim of the determination of the crystal structure is to increase the understanding of this industrially significant enzyme.
Maksimainen
Mirko
M
Department of Chemistry, University of Joensuu, Finland.
Timoharju
Tommi
T
Kallio
Johanna M
JM
Hakulinen
Nina
N
Turunen
Ossi
O
Rouvinen
Juha
J
D002852:Chromatography, Ion Exchange; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D011487:Protein Conformation; D014242:Trichoderma / Q000201:enzymology*; D014961:X-Ray Diffraction; D001616:beta-Galactosidase / Q000737:chemistry* / Q000302:isolation & purification
D001616:beta-Galactosidase