title: Preliminary crystallographic data for Pneumocystis carinii dihydrofolate reductase.
abstract: 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.
authors: Wellcome Research Laboratories, Beckenham, Kent, U.K.
authors: D K
authors: DK
authors: Stammers
authors: C
authors: C
authors: Delves
authors: S
authors: S
authors: Ballantine
authors: E Y
authors: EY
authors: Jones
authors: D I
authors: DI
authors: Stuart
authors: A
authors: A
authors: Achari
authors: P K
authors: PK
authors: Bryant
authors: J N
authors: JN
authors: Champness
mesh_terms: D017088:AIDS-Related Opportunistic Infections / Q000382:microbiology; D005798:Genes, Bacterial; D006801:Humans; D009249:NADP / Q000378:metabolism; D011010:Pneumocystis / Q000201:enzymology*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014295:Trimethoprim / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D009249:NADP; D014295:Trimethoprim; D013762:Tetrahydrofolate Dehydrogenase