Crystallization and preliminary X-ray study of Pk--REC from a hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1.
Pk-REC is a protein which binds to DNA and catalyzes the central step of recombination and repair. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG as a precipitant. Two orthorhombic crystal forms I and II with the same space group P2(1)2(1)2(1) were obtained at pH 8.0 using PEG 3000 and PEG 550 monomethylether, respectively. The unit-cell parameters were a = 151, b = 174, c = 241 A for form I and a = 151, b = 176, c = 300 A for form II, indicating that the asymmetric unit contains more than 20 molecules.
Harata
K
K
Biomolecules Department, National Institute of Bioscience and Human Technology, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan. harata@nibh.go.jp
Ishii
N
N
Rashid
N
N
Morikawa
M
M
Imanaka
T
T
D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D011092:Polyethylene Glycols; D019711:Pyrococcus / Q000235:genetics*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D019843:Archaeal Proteins; C103757:Pk-REC protein, Pyrococcus sp.; D011994:Recombinant Proteins; D011092:Polyethylene Glycols