Crystallization and preliminary X-ray analysis of endoglucanase fromPyrococcus horikoshii

Abstract

Structural information on hyperthermostable cellulases is required for bioprocess applications in the transformation of biomass. Crystals were obtained of a C-terminally five-amino-acid truncated hyperthermostable endoglucanase (family 5) from the archaeon Pyrococcus horikoshii. The truncated form of this enzyme showed similar enzymatic properties to the wild-type protein. The enzyme was crystallized by the sitting-drop vapour-diffusion method using ethanol as precipitant at 296 K. An X-ray diffraction data set was collected to 1.78 A resolution at 100 K. The crystals belonged to space group P4(1)2(1)2 or P4(3)2(1)2.