title: Crystallization and preliminary crystallographic analysis of the catalytic domain cellobiohydrolase I from Talaromyces emersonii.
abstract: Cellobiohydrolase IB is the first native enzyme from the filamentous fungus Talaromyces emersonii to be crystallized. It is a highly thermostable exo-acting enzyme. The native enzyme (MW = 56 kDa) was crystallized using the hanging-drop vapour-diffusion method with ammonium phosphate (dibasic) as a precipitant at pH 8.5. The crystal belongs to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 74.43, c = 176.92 A, and diffracted to 1.77 A resolution at room temperature.
authors.affiliation: Department of Chemistry, National University of Ireland, Galway, Ireland.
authors.forename: Alice
authors.initials: A
authors.lastname: Grassick
authors.forename: Gabriel
authors.initials: G
authors.lastname: Birrane
authors.forename: Maria
authors.initials: M
authors.lastname: Tuohy
authors.forename: Patrick
authors.initials: P
authors.lastname: Murray
authors.forename: Timothy
authors.initials: T
authors.lastname: Higgins
mesh_terms: D001665:Binding Sites; D020134:Catalytic Domain; D043366:Cellulose 1,4-beta-Cellobiosidase / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D010710:Phosphates; D032901:Talaromyces / Q000737:chemistry*
chemical_list: D005656:Fungal Proteins; D010710:Phosphates; C024788:ammonium phosphate; D043366:Cellulose 1,4-beta-Cellobiosidase