Crystallization and preliminary crystallographic analysis of the catalytic domain cellobiohydrolase I from Talaromyces emersonii.
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.
Grassick
Alice
A
Department of Chemistry, National University of Ireland, Galway, Ireland.
Birrane
Gabriel
G
Tuohy
Maria
M
Murray
Patrick
P
Higgins
Timothy
T
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*
D005656:Fungal Proteins; D010710:Phosphates; C024788:ammonium phosphate; D043366:Cellulose 1,4-beta-Cellobiosidase