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.