title: Crystallization and preliminary X-ray analysis of a fungal endoglucanase I.
abstract: An endoglucanase I (EG1) from a fungal source (Humicola insolens) has been crystallized in a number of forms suitable for X-ray diffraction analysis. Four crystal forms have been grown from various precipitants using vapour phase diffusion methods in hanging drops. Three of these crystal forms diffract to beyond 2.5 A resolution. Two forms, obtained from ammonium sulphate at pH 5.4, or 8.0, grow as tetragonal bipyramids in space group P4(1)22 or P4(3)22, with approximate cell dimensions a = b = 102 A, c = 282 A. The other crystal forms were grown from polyethylene glycol 8000 at pH 8.0. One grows as monoclinic plates, space group P2(1), with cell dimensions a = 66.9 A, b = 75.2 A, c = 86.9 A and beta = 102.9 degrees and the other as long hexagonal rods in space group P6(1)22 or P6(5)22, with cell dimensions a = b = 119 A, c = 83 A.
authors: Department of Chemistry, University of York, Heslington, England.
authors: G
authors: G
authors: Davies
authors: S
authors: S
authors: Tolley
authors: K
authors: K
authors: Wilson
authors: M
authors: M
authors: Schülein
authors: H F
authors: HF
authors: Wöldike
authors: G
authors: G
authors: Dodson
mesh_terms: D043366:Cellulose 1,4-beta-Cellobiosidase; D003460:Crystallization; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D007526:Isoelectric Point; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; D043366:Cellulose 1,4-beta-Cellobiosidase