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Crystallization and preliminary X‐ray diffraction analysis of Hypocrea jecorina Cel7A in two new crystal forms
Author(s) -
Bodenheimer Annette M.,
Cuneo Matthew J.,
Swartz Paul D.,
He Junhong,
O'Neill Hugh M.,
Myles Dean A. A.,
Evans Barbara R.,
Meilleur Flora
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14008851
Subject(s) - hypocrea , crystallization , crystallography , linker , residue (chemistry) , chemistry , diffraction , crystal structure , materials science , cellulose , physics , cellulase , optics , organic chemistry , trichoderma reesei , computer science , operating system
Cel7A (previously known as cellobiohydrolase I) from Hypocrea jecorina was crystallized in two crystalline forms, neither of which have been previously reported. Both forms co‐crystallize under the same crystallization conditions. The first crystal form belonged to space group C 2, with unit‐cell parameters a = 152.5, b = 44.9, c = 57.6 Å, β = 101.2°, and diffracted X‐rays to 1.5 Å resolution. The second crystal form belonged to space group P 6 3 22, with unit‐cell parameters a = b ≃ 155, c ≃ 138 Å, and diffracted X‐rays to 2.5 Å resolution. The crystals were obtained using full‐length Cel7A, which consists of a large 434‐residue N‐terminal catalytic domain capable of cleaving cellulose, a 27‐residue flexible linker and a small 36‐residue C‐terminal carbohydrate‐binding module (CBM). However, a preliminary analysis of the electron‐density maps suggests that the linker and CBM are disordered in both crystal forms. Complete refinement and structure analysis are currently in progress.