Crystallization of RusA Holliday junction resolvase from Escherichia coli.
Crystals of the Escherichia coli Holliday junction resolvase RusA have been obtained using the hanging-drop method and characterized. The crystals have a primitive monoclinic form and belong to space group P2(1). The V(M) value suggests the presence of two copies of the monomer in the asymmetric unit. A full three-wavelength MAD data collection on a selenomethionine-incorporated form has been undertaken and structure determination is under way using data collected to 2.1 A resolution.
Muranova
Tatyana A
TA
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield S10 2TN, England.
Sedelnikova
Svetlana E
SE
Leonard
Philip M
PM
Pasquo
Alessandra
A
Bolt
Edward L
EL
Lloyd
Robert G
RG
Rafferty
John B
JB
D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D045565:Holliday Junction Resolvases / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012645:Selenomethionine / Q000737:chemistry
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D012645:Selenomethionine; D045565:Holliday Junction Resolvases; C112057:RusA protein, E coli