Preliminary crystallographic data for Pneumocystis carinii dihydrofolate reductase.
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.
Stammers
D K
DK
Wellcome Research Laboratories, Beckenham, Kent, U.K.
Delves
C
C
Ballantine
S
S
Jones
E Y
EY
Stuart
D I
DI
Achari
A
A
Bryant
P K
PK
Champness
J N
JN
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
D011994:Recombinant Proteins; D009249:NADP; D014295:Trimethoprim; D013762:Tetrahydrofolate Dehydrogenase