Abstract
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 |
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Pages (from-to) | 775-777 |
Number of pages | 3 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 56 |
Issue number | 6 |
DOIs | |
State | Published - 2000 |