Crystallization and preliminary X-ray analysis of endoglucanase from Pyrococcus horikoshii.
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.
Kim
Han-Woo
HW
National Institute of Advanced Industrial Science and Technology, 1-18-31, Midorigaoka, Ikeda, Osaka 563-8577, Japan.
Mino
Koshiki
K
Ishikawa
Kazuhiko
K
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry*; D002480:Cellulase / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D016415:Sequence Alignment
D019843:Archaeal Proteins; D002480:Cellulase