1998
Substrate Channeling and Domain−Domain Interactions in Bifunctional Thymidylate Synthase−Dihydrofolate Reductase †
Liang P, Anderson K. Substrate Channeling and Domain−Domain Interactions in Bifunctional Thymidylate Synthase−Dihydrofolate Reductase †. Biochemistry 1998, 37: 12195-12205. PMID: 9724533, DOI: 10.1021/bi9803168.Peer-Reviewed Original ResearchConceptsDHFR active siteActive siteTS active siteCrystal structureTransient kinetic analysisEnzyme active siteBifunctional TS-DHFRProtein surfaceTS-DHFRKinetics of substrateReductase enzymeSingle polypeptide chainKinetic analysisDihydrofolateThymidylate synthasePolypeptide chainSubstrateEnzymeStructureDomain-domain interactionsSpecies of protozoaInteractionKineticsL. majorChain
1995
Crystallization and preliminary X‐ray investigation of the recombinant Trypanosoma brucei rhodesiense calmodulin
El‐Sayed N, Patton C, Harkins P, Fox R, Anderson K. Crystallization and preliminary X‐ray investigation of the recombinant Trypanosoma brucei rhodesiense calmodulin. Proteins Structure Function And Bioinformatics 1995, 21: 354-357. PMID: 7567957, DOI: 10.1002/prot.340210409.Peer-Reviewed Original ResearchConceptsPreliminary X-ray investigationUnit cell dimensionsMolecular replacement methodX-ray investigationsSpace groupAsymmetric unitCrystal structureCell dimensionsRecombinant calmodulinMolecular massCrystalUnit cellTrypanosoma brucei rhodesienseVapor diffusionReplacement methodM cacodylate bufferCalmodulinStructure