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Crystallization and preliminary X-ray analysis of endoglucanase from Pyrococcus 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.

SUBMITTER: Kim HW

PROVIDER: S-EPMC2593689 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of endoglucanase from Pyrococcus horikoshii.

Kim Han-Woo HW Mino Koshiki K Ishikawa Kazuhiko K

Acta crystallographica. Section F, Structural biology and crystallization communications 20081128 Pt 12

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 diff ...[more]

PMID: 19052378

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