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Dihydrofolate reductase from Pneumocystis carinii has been crystallized in a form suitable for high resolution X-ray diffraction studies. Recombinant enzyme that had been refolded following solubilization in guanidinium hydrochloride was crystallized as both a ternary complex with the cofactor NADPH and the inhibitor trimethoprim as well as a binary complex with NADPH. The two types of complex crystallized isomorphously from polyethylene glycol using sitting-drop vapour diffusion. The crystals were of space group P2(1) with unit cell parameters, a = 69.9 A, b = 43.6 A, c = 37.6 A, beta = 117.7 degrees, with one molecule per asymmetric unit. The crystals diffracted to 1.8 A resolution.

Original publication




Journal article


J Mol Biol

Publication Date





679 - 680


AIDS-Related Opportunistic Infections, Genes, Bacterial, Humans, NADP, Pneumocystis, Protein Binding, Recombinant Proteins, Tetrahydrofolate Dehydrogenase, Trimethoprim, X-Ray Diffraction