Crystallization and preliminary X-ray diffraction analysis of the catalytic domain of Cex, an exo-β-1,4-glucanase and β-1,4-xylanase from the bacterium Cellulomonas fimi

• Published in: Journal of molecular biology Vol. 228; no. 2; pp. 693 - 695
• Main Authors: Bedarkar, Sudhir, Gilkes, Neil R., Kilburn, Douglas G., Kwan, Emily, Rose, David R., Miller, Robert C., Warren, R.Antony J., Withers, Stephen G.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 20.11.1992; Elsevier
• Subjects: Actinomycetales - enzymology; beta-Glucosidase - chemistry; Biological and medical sciences; Cellulomonas fimi; Crystalline structure; Crystallization; Endo-1,4-beta Xylanases; Fundamental and applied biological sciences. Psychology; Glucan 1,4-beta-Glucosidase; glucanase; Glycoside Hydrolases - chemistry; Molecular biophysics; Structure in molecular biology; X-ray crystallography; X-Ray Diffraction; xylanase; Unit cell; Exo-1,4-β-D-glucosidase; Enzyme; Cellulomonas fimi; Crystallization; Bacteria; Actinomycetes; Catalytic site; Exo-1,4-β-D-xylosidase; X ray diffraction
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/0022-2836(92)90852-B

Single crystals of the catalytic domain of Cex, an exo-β-1,4-glucanase and β-1,4-xylanase from the cellulolytic bacterium Cellulomonas fimi, have been grown in the presence of polyethylene glycol 4000 using the vapour diffusion technique. The crystals, which diffract to better than 2.0 Å resolution, belong to space group P4 12 12 or P4 32 12 and have cell constants: a = b = 88.21 A ̊ , c = 81.10 A ̊ ; α = β = γ = 90 °.