Crystallization and preliminary crystallographic analysis of a DNA (cytosine-5)-methyltransferase from Haemophilus aegyptius bound covalently to DNA.
A DNA (cytosine)-5-methyltransferase from Haemophilus aegyptius (M.Hae III), which catalyzes methyl transfer from S-adenosyl-L-methionine to DNA, has been crystallized as a covalent complex with a suicide oligonucleotide substrate. Crystals of the co-complex were grown by vapor diffusion with hanging droplets, using polyethylene glycol 3500 as the precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1); the unit cell parameters are a = 57.6 A, b = 108.0 A, c = 155.8 A with two protein-DNA complexes in the asymmetric unit. Complete sets of native and derivative data have been collected to 2.7 A using a laboratory source.
Reinisch
K M
KM
Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.
Chen
L
L
Verdine
G L
GL
Lipscomb
W N
WN
D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism*; D004248:DNA (Cytosine-5-)-Methyltransferases / Q000737:chemistry* / Q000378:metabolism*; D003841:Deoxycytidine / Q000031:analogs & derivatives; D006190:Haemophilus / Q000201:enzymology*; D008969:Molecular Sequence Data; D011089:Polydeoxyribonucleotides / Q000138:chemical synthesis; D011485:Protein Binding
D011089:Polydeoxyribonucleotides; D003841:Deoxycytidine; D004247:DNA; D004248:DNA (Cytosine-5-)-Methyltransferases; C007746:5-fluoro-2'-deoxycytidine