Crystallization and preliminary X-ray analysis of RecG, a replication-fork reversal helicase from Thermotoga maritima complexed with a three-way DNA junction.
The monomeric 3'-5' helicase RecG from the thermophilic bacterium Thermotoga maritima has been crystallized in complex with a three-way DNA junction, the preferred physiological substrate. The crystals were obtained by hanging-drop vapour diffusion. The crystals belong to space group C2, with unit-cell parameters a = 133.7, b = 144.6, c = 84.0 A, beta = 113.8 degrees. Native data to a resolution of 3.25 A were collected from crystals flash-cooled to 100 K.
Singleton
M R
MR
Imperial Cancer Research Fund, Clare Hall Laboratories, Blanche Lane, South Mimms, Hertfordshire EN6 3LD, England.
Scaife
S
S
Raven
N D
ND
Wigley
D B
DB
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D020124:Thermotoga maritima / Q000201:enzymology*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C071446:RecG protein, E coli; D004247:DNA