1990
The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution
Sanderson M, Freemont P, Rice P, Goldman A, Hatfull G, Grindley N, Steitz T. The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution. Cell 1990, 63: 1323-1329. PMID: 2175678, DOI: 10.1016/0092-8674(90)90427-g.Peer-Reviewed Original Research
1984
Mutants of the γδ resolvase: A genetic analysis of the recombination function
Newman B, Grindley N. Mutants of the γδ resolvase: A genetic analysis of the recombination function. Cell 1984, 38: 463-469. PMID: 6088082, DOI: 10.1016/0092-8674(84)90501-4.Peer-Reviewed Original ResearchConceptsAmino acid amino-terminal domainAmino-terminal domainDifferent amino acid substitutionsSite-specific recombinationGamma delta transposonAmino acid substitutionsRecombination functionsTransposon genesIndependent mutantsCatalytic domainRelated recombinasesGenetic analysisDistinct residuesΓδ resolvaseMutantsAcid substitutionsResolvaseRegulatory propertiesCrossover sitesAmino acidsResolvase proteinCointegrate resolutionRecombinasesTransposonGenes
1980
THE PRIMARY STRUCTURE OF DNA POLYMERASE I OF E. COLI11This work was supported by Health and Research Services Foundation grant V-34 (to NDFG), NIH grant GM24688 (to WSK) and ACS Faculty Research Award 198 (to WSK).
Joyce C, Kelley W, Brown W, Grindley N. THE PRIMARY STRUCTURE OF DNA POLYMERASE I OF E. COLI11This work was supported by Health and Research Services Foundation grant V-34 (to NDFG), NIH grant GM24688 (to WSK) and ACS Faculty Research Award 198 (to WSK). 1980, 589-596. DOI: 10.1016/b978-0-12-048850-6.50054-5.Peer-Reviewed Original ResearchDNA polymerase IPolymerase IE. coli polA geneAmino acid sequenceHalf-cystine residuesProteolytic cleavage sitesResidues 342Sequence comparisonDNA polymerase I.DNA sequencesResidue 323Acid sequencePolymerase I.PolA geneNative enzymeCleavage siteAmino acidsSequenceGenesProteinMutationsAllelesEnzymeResiduesTrp