Crystallization and preliminary X-ray crystallographic analysis of the RecR protein from Deinococcus radiodurans, a member of the RecFOR DNA-repair pathway.
The RecR protein plays a key role in the RecFOR pathway of recombination, which is necessary for the repair of ssDNA gaps. RecR from Deinococcus radiodurans has been overexpressed in Escherichia coli and crystallized at 297 K using polyethylene glycol 1000 as a precipitant. X-ray diffraction data to 2.90 A resolution have been collected at 100 K using Cu Kalpha X-rays from a mercury-soaked crystal. The crystal belongs to space group C222(1), with unit-cell parameters a = 106.96, b = 122.25, c = 156.01 A. The asymmetric unit contains four monomers of RecR, with a crystal volume per protein weight (V(M)) of 2.57 A(3) Da(-1) and a solvent content of 51.0%.
Lee
Byung Il
BI
Structural Proteomics Laboratory, Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, South Korea.
Kim
Kyoung Hoon
KH
Shim
Sun Mi
SM
Ha
Kyung Soo
KS
Yang
Jin Kuk
JK
Yoon
Hye-Jin
HJ
Ha
Jun Yong
JY
Suh
Se Won
SW
D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods*; D004260:DNA Repair; D004277:DNA, Single-Stranded / Q000737:chemistry; D034301:Deinococcus / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D008027:Light; D008628:Mercury / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011995:Recombination, Genetic; D012542:Scattering, Radiation; D012997:Solvents; D013696:Temperature; D014965:X-Rays
D001426:Bacterial Proteins; D004277:DNA, Single-Stranded; D029968:Escherichia coli Proteins; C489318:RecR protein, E coli; D012997:Solvents; C065831:RecR protein, Bacteria; D008628:Mercury