Preliminary crystallographic data for Pneumocystis carinii dihydrofolate reductase
| Autor: | J.N. Champness, David I. Stuart, S.P. Ballantine, C.J. Delves, David K. Stammers, E Y Jones, A Achari, P.K. Bryant |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Stereochemistry
Polyethylene glycol Trimethoprim Cofactor chemistry.chemical_compound X-Ray Diffraction Structural Biology Dihydrofolate reductase Humans Molecular Biology Ternary complex chemistry.chemical_classification AIDS-Related Opportunistic Infections biology Pneumocystis Resolution (electron density) Recombinant Proteins Tetrahydrofolate Dehydrogenase Crystallography Enzyme Pneumocystis carinii chemistry Genes Bacterial X-ray crystallography biology.protein NADP Protein Binding |
| Popis: | Dihydrofolate reductase from Pneumocytis 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 P 2 1 with unit cell parameters, a = 69·9 A, b = 43·6 A, c = 37·6 A, β = 117·7°, with one molecule per asymmetric unit. The crystals diffracted to 1·8 A resolution. |
| Databáze: | OpenAIRE |
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