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‐c...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-11, Vol.57 (11), p.1695-1696
Main Authors: Singleton, Martin R., Scaife, Sarah, Raven, Neil D., Wigley, Dale B.
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Crystallization
Crystallography, X-Ray
DNA - chemistry
DNA - metabolism
Escherichia coli Proteins
Nucleic Acid Conformation
Protein Conformation
replication-fork reversal helicases
Thermotoga maritima - enzymology
three-way DNA junctions
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Summary: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 Å, β = 113.8°. Native data to a resolution of 3.25 Å were collected from crystals flash‐cooled to 100 K.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444901013105