Preliminary X-ray analysis of cellobiohydrolase Cel7B from Melanocarpus albomyces

Cellobiohydrolases are enzymes that cleave off cellobiose units from cellulose chains in a processive manner. Melanocarpus albomyces Cel7B is a thermostable single‐module cellobiohydrolase that has relatively low activity on small soluble substrates at room temperature. It belongs to glycoside hydro...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-09, Vol.63 (9), p.754-757
Main Authors: Parkkinen, Tarja, Koivula, Anu, Vehmaanperä, Jari, Rouvinen, Juha
Format: Article
Language:English
Subjects:
Ascomycota - enzymology
cellobiohydrolase
cellulase
CELLULOSE
Cellulose 1,4-beta-Cellobiosidase - chemistry
Cellulose 1,4-beta-Cellobiosidase - isolation & purification
Cellulose 1,4-beta-Cellobiosidase - metabolism
CHAINS
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
Crystallization Communications
CRYSTALS
DIFFUSION
Fungal Proteins - chemistry
Fungal Proteins - isolation & purification
Kinetics
MONOMERS
RESOLUTION
Scattering, Radiation
SPACE GROUPS
SUBSTRATES
SYNCHROTRON RADIATION
TWINNING
X-RAY DIFFRACTION
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Summary:Cellobiohydrolases are enzymes that cleave off cellobiose units from cellulose chains in a processive manner. Melanocarpus albomyces Cel7B is a thermostable single‐module cellobiohydrolase that has relatively low activity on small soluble substrates at room temperature. It belongs to glycoside hydrolase family 7, which includes endo‐β‐1,4‐glucanases and cellobiohydrolases. Cel7B was crystallized using the hanging‐drop vapour‐diffusion method and streak‐seeding. The crystals belonged to space group P21, with unit‐cell parameters a = 50.9, b = 94.5, c = 189.8 Å, β = 90.0° and four monomers in the asymmetric unit. Analysis of the intensity statistics showed that the crystals were pseudo‐merohedrally twinned, with a twinning fraction of 0.37. X‐ray diffraction data were collected at 1.6 Å resolution using synchrotron radiation.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309107034458