Crystallization and preliminary X-ray crystallographic analysis of Aart, a designed six-finger zinc-finger peptide, bound to DNA.
Crystals of a designed six-finger zinc-finger protein, Aart, bound to a 22-base-pair duplex DNA containing a consensus binding site have been obtained. Crystals grew by hanging-drop vapor diffusion from solutions containing polyethylene glycol 4000 as the precipitating agent. The irregularly shaped crystals belong to space group P1, with unit-cell parameters a = 41.95, b = 71.76, c = 74.73 A, alpha = 100.87, beta = 96.22, gamma = 106.33 degrees . There are most likely to be two protein-DNA complexes in the asymmetric unit. A complete native data set has been collected from a high-energy synchrotron source to a resolution of 2.95 A at 100 K, with an Rmerge of 9.3%.
Crotty
Justin W
JW
Department of Chemistry, University of Arizona, Tucson, AZ 85721, USA.
Etzkorn
Christopher
C
Barbas
Carlos F
CF
Segal
David J
DJ
Horton
Nancy C
NC
D000595:Amino Acid Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics; D011092:Polyethylene Glycols; D014835:Volatilization; D014961:X-Ray Diffraction; D016335:Zinc Fingers
D004268:DNA-Binding Proteins; D011092:Polyethylene Glycols