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 P4122 (or P4322), with unit-cell parameters a = b = 61.14, c = 123.23 Å under cryogenic conditions. The asymmetric unit contains a single subunit, with a corresponding V(m) of 2.65 Å3 Da-1 and a solvent content of 53.6%. Native data have been collected from a crystal to 1.9 Å resolution using synchrotron X-rays.
|Original language||English (US)|
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - 2000|
ASJC Scopus subject areas
- Structural Biology