Crystallization and preliminary X-ray crystallographic analysis of a Trichoderma reesei beta-mannanase from glycoside hydrolase family 5.
Crystals of the catalytic core domain of a Trichoderma reesei beta-mannanase belonging to glycoside hydrolase family 5 have been grown by the sitting-drop method at room temperature using ammonium sulfate as precipitant. The crystals grow as thin colourless plates and belong to space group P21, with unit-cell parameters a = 50.0, b = 54.3, c = 60.2 A, beta = 111.3 degrees, and have a single monomer of mannanase in the asymmetric unit. Native data to 2.0 A resolution have been collected at room temperature using synchrotron radiation. Data for a platinum derivative have been collected to 1.65 A at 110 K in a very short time at the CCLRC Daresbury synchrotron source, using a charge-coupled device (CCD) as detector.
Sabini
E
E
Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, England.
Brzozowski
A M
AM
Dauter
M
M
Davies
G J
GJ
Wilson
K S
KS
Paloheimo
M
M
Suominen
P
P
Siika-Aho
M
M
Penttilä
M
M
D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification; D008361:Mannosidases / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification; D014242:Trichoderma / Q000201:enzymology*; D044902:beta-Mannosidase
D005656:Fungal Proteins; D008361:Mannosidases; D044902:beta-Mannosidase