2016
Data publication with the structural biology data grid supports live analysis
Meyer PA, Socias S, Key J, Ransey E, Tjon EC, Buschiazzo A, Lei M, Botka C, Withrow J, Neau D, Rajashankar K, Anderson KS, Baxter RH, Blacklow SC, Boggon TJ, Bonvin AM, Borek D, Brett TJ, Caflisch A, Chang CI, Chazin WJ, Corbett KD, Cosgrove MS, Crosson S, Dhe-Paganon S, Di Cera E, Drennan CL, Eck MJ, Eichman BF, Fan QR, Ferré-D'Amaré AR, Christopher Fromme J, Garcia KC, Gaudet R, Gong P, Harrison SC, Heldwein EE, Jia Z, Keenan RJ, Kruse AC, Kvansakul M, McLellan JS, Modis Y, Nam Y, Otwinowski Z, Pai EF, Pereira PJ, Petosa C, Raman CS, Rapoport TA, Roll-Mecak A, Rosen MK, Rudenko G, Schlessinger J, Schwartz TU, Shamoo Y, Sondermann H, Tao YJ, Tolia NH, Tsodikov OV, Westover KD, Wu H, Foster I, Fraser JS, Maia FR, Gonen T, Kirchhausen T, Diederichs K, Crosas M, Sliz P. Data publication with the structural biology data grid supports live analysis. Nature Communications 2016, 7: 10882. PMID: 26947396, PMCID: PMC4786681, DOI: 10.1038/ncomms10882.Peer-Reviewed Original ResearchMeSH KeywordsCrystallography, X-RayDatabases, GeneticInternetMacromolecular SubstancesPublicationsSoftwareConceptsData gridData publicationData setsGlobal data accessPrimary experimental data setsBiomedical data setsData accessExperimental data setsImage dataDissemination systemPilot collectionProcessing methodsGridSetData analysisAccessParadigm shiftDynamic bodyScientific publicationsSBDGServicesInformationCrystallographic data sets
1999
Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡
Sachpatzidis A, Dealwis C, Lubetsky J, Liang P, Anderson K, Lolis E. Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡. Biochemistry 1999, 38: 12665-12674. PMID: 10504236, DOI: 10.1021/bi9907734.Peer-Reviewed Original ResearchMeSH KeywordsCrystallography, X-RayEnzyme InhibitorsHydrogen BondingModels, MolecularOrganophosphonatesTryptophan SynthaseConceptsTransition stateShort hydrogen bondsTryptophan synthaseHigh conformational flexibilityTetrahedral transition stateTransition state analogueMechanism of catalysisEnzyme-inhibitor complexStructure-based approachPhosphonate oxygenIndole-3-glycerol phosphateHydroxyl oxygenHydrogen bondsSulfur atomsActive siteC3 atomC2 atomCrystal structureConformational flexibilityCrystallographic studiesInhibitor bindingConformation changeAtomsNew herbicidesGlu-49
1998
Loop Closure and Intersubunit Communication in Tryptophan Synthase † , ‡
Schneider T, Gerhardt E, Lee M, Liang P, Anderson K, Schlichting I. Loop Closure and Intersubunit Communication in Tryptophan Synthase † , ‡. Biochemistry 1998, 37: 5394-5406. PMID: 9548921, DOI: 10.1021/bi9728957.Peer-Reviewed Original ResearchConceptsBeta-active siteMechanism of allosteric activationAlpha-active siteAlpha subunitTryptophan synthase alpha2beta2 complexPyridoxal phosphateCofactor pyridoxal phosphatePresence of serineSalmonella typhimuriumIntersubunit communicationTryptophan synthaseAllosteric activationAlpha2beta2 complexAllosteric propertiesAlpha-reactionBeta-reactionBeta subunitStructural basisAminoacrylate intermediateAminoacrylatePathwayBindingSitesTryptophanSerine
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 ResearchMeSH KeywordsAnimalsBinding SitesCalciumCalmodulinCrystallizationCrystallography, X-RayElectrophoresis, Polyacrylamide GelRecombinant ProteinsTrypanosoma brucei rhodesienseConceptsPreliminary X-ray investigationUnit cell dimensionsMolecular replacement methodX-ray investigationsSpace groupAsymmetric unitCrystal structureCell dimensionsRecombinant calmodulinMolecular massCrystalUnit cellTrypanosoma brucei rhodesienseVapor diffusionReplacement methodM cacodylate bufferCalmodulinStructure