Overexpression, crystallization and preliminary X-ray crystallographic analysis of dihydrofolate reductase from bacteriophage T4.
Dihydrofolate reductase (DHFR) from bacteriophage T4 is a homodimer consisting of 193-residue subunits. It has been crystallized in the presence of the cofactor (NADPH) and an inhibitor (aminopterin) at 296 K using sodium chloride as precipitant. The crystals are tetragonal, belonging to the space group P4(1)22 (or P4(3)22), with unit-cell parameters a = b = 61.14, c = 123.23 A under cryogenic conditions. The asymmetric unit contains a single subunit, with a corresponding V(m) of 2.65 A(3) Da(-1) and a solvent content of 53. 6%. Native data have been collected from a crystal to 1.9 A resolution using synchrotron X-rays.
Oh
Y K
YK
Department of Chemistry, College of Natural Sciences, Seoul National University, South Korea.
Moon
J
J
Lee
J Y
JY
Cho
S W
SW
Shin
W
W
Suh
S W
SW
D017122:Bacteriophage T4 / Q000201:enzymology* / Q000235:genetics*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003625:Data Collection; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000821:virology; D015964:Gene Expression Regulation, Bacterial; D015967:Gene Expression Regulation, Viral; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D017356:Synchrotrons; D013762:Tetrahydrofolate Dehydrogenase / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification
D011994:Recombinant Proteins; D013762:Tetrahydrofolate Dehydrogenase