Literature DB >> 10771438

Crystallization and preliminary X-ray study of Pk--REC from a hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1.

K Harata1, N Ishii, N Rashid, M Morikawa, T Imanaka.   

Abstract

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.

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Year:  2000        PMID: 10771438     DOI: 10.1107/s0907444900002821

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Structure of RadB recombinase from a hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1: an implication for the formation of a near-7-fold helical assembly.

Authors:  Toshihiko Akiba; Noriyuki Ishii; Naeem Rashid; Masaaki Morikawa; Tadayuki Imanaka; Kazuaki Harata
Journal:  Nucleic Acids Res       Date:  2005-06-13       Impact factor: 16.971

  1 in total

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