Crystallization and X-ray diffraction analysis of a catalytic domain of hyperthermophilic chitinase from Pyrococcus furiosus.
The crystallization and preliminary X-ray diffraction analysis of a catalytic domain of chitinase (PF1233 gene) from the hyperthermophilic archaeon Pyrococcus furiosus is reported. The recombinant protein, prepared using an Escherichia coli expression system, was crystallized by the hanging-drop vapour-diffusion method. An X-ray diffraction data set was collected at the undulator beamline BL44XU at SPring-8 to a resolution of 1.50 angstroms. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 90.0, b = 92.8, c = 107.2 angstroms.
Mine
Shouhei
S
National Institute of Advanced Industrial Science and Technology (AIST), 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577, Japan.
Nakamura
Tsutomu
T
Hirata
Kunio
K
Ishikawa
Kazuhiko
K
Hagihara
Yoshihisa
Y
Uegaki
Koichi
K
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D020134:Catalytic Domain; D002688:Chitinases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology; D008969:Molecular Sequence Data; D020027:Pyrococcus furiosus / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D013816:Thermodynamics; D014961:X-Ray Diffraction
D019843:Archaeal Proteins; D011994:Recombinant Proteins; D002688:Chitinases