Crystallization and preliminary crystallographic analysis of Escherichia coli DNA photolyase.
DNA photolyase from Escherichia coli (M(r) 54,000) consists of a polypeptide chain of 471 amino acids and the non-covalently bound cofactors methenyltetrahydrofolate (MTHF) and flavin adenine dinucleotide (FADH2). Two crystal forms of the enzyme were obtained; both have symmetry of space group P1. Form I has the unit cell dimensions a = 89.4 A, b = 97.3 A, c = 62.1 A, alpha = 108.3 degrees, beta = 97.4 degrees and gamma = 90.0 degrees. Diffraction from this form extends beyond 3 A resolution, but the crystals are radiation-sensitive and difficult to reproduce. Form II has the unit cell dimensions a = 62.6 A, b = 72.2 A, c = 58.5 A, alpha = 99.1 degrees, beta = 101.5 degrees and gamma = 72.0 degrees; most likely, the unit cell contains two molecules. High diffraction quality and reproducibility make form II suitable for structure analysis.
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.
H W
HW
Park
A
A
Sancar
J
J
Deisenhofer
D003460:Crystallization; D004255:Deoxyribodipyrimidine Photo-Lyase / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology*; D005182:Flavin-Adenine Dinucleotide / Q000031:analogs & derivatives; D013763:Tetrahydrofolates; D014961:X-Ray Diffraction
D013763:Tetrahydrofolates; D005182:Flavin-Adenine Dinucleotide; C029276:flavin semiquinone; C018092:5,10-methenyltetrahydrofolate; D004255:Deoxyribodipyrimidine Photo-Lyase