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P184
P185
Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysomeProtein Structures Forming the Shell of Primitive Bacterial OrganellesMultiple crystal structures of actin dimers and their implications for interactions in the actin filamentConnecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxinThe genomics of disulfide bonding and protein stabilization in thermophilesThe structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathwayThe crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bondsCrystal structure of human L-isoaspartyl methyltransferaseThe crystal structure of a cyanobacterial water-soluble carotenoid binding proteinAmyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALSThe 1.6 A resolution structure of Fe-superoxide dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatusThe crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosisStructural and EPR characterization of the soluble form of cytochrome c-550 and of the psbV2 gene product from the cyanobacterium Thermosynechococcus elongatusStructure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15Discovery of a Thermophilic Protein Complex Stabilized by Topologically Interlinked ChainsStructure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803Atomic-level models of the bacterial carboxysome shellStructures and Functional Implications of an AMP-Binding Cystathionine β-Synthase Domain Protein from a Hyperthermophilic ArchaeonStructure of the PduU shell protein from the Pdu microcompartment of SalmonellaInsights from multiple structures of the shell proteins from the β-carboxysomeDetermining the DUF55-domain structure of human thymocyte nuclear protein 1 from crystals partially twinned by tetartohedryAnalysis of lattice-translocation disorder in the layered hexagonal structure of carboxysome shell protein CsoS1CDirected Evolution and Structural Characterization of a Simvastatin SynthaseStructure and mechanisms of a protein-based organelle in Escherichia coliDetermination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallographyStructural Insight into the Mechanisms of Transport across the Salmonella enterica Pdu Microcompartment ShellTotal chemical synthesis and X-ray structure of kaliotoxin by racemic protein crystallographyStructure and folding of a designed knotted proteinSynthetic symmetrization in the crystallization and structure determination of CelA fromThermotoga maritimaAn approach to crystallizing proteins by metal-mediated synthetic symmetrizationStructural and Biochemical Characterization of the Salicylyl-acyltranferase SsfX3 from a Tetracycline Biosynthetic PathwayInward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibitionBacterial microcompartment shells of diverse functional types possess pentameric vertex proteinsStructure and flexibility of nanoscale protein cages designed by symmetric self-assembly.Structure of a 16-nm cage designed by using protein oligomersComputational Design of Self-Assembling Protein Nanomaterials with Atomic Level AccuracySplit green fluorescent protein as a modular binding partner for protein crystallizationA challenging interpretation of a hexagonally layered protein structureStructure and Identification of a Pterin Dehydratase-like Protein as a Ribulose-bisphosphate Carboxylase/Oxygenase (RuBisCO) Assembly Factor in the α-CarboxysomeStructure of Dihydromethanopterin Reductase, a Cubic Protein Cage for Redox Transfer
P50
Q21092759-D7945C39-03E1-45B9-9C2D-46CCF336FFD1Q22299353-C3C8E8B3-7442-402D-A9A1-92AB13217A8BQ24645201-2F4675B4-569D-4063-BEF0-F9AE32FC6386Q24653785-51EBDCEC-969C-44DC-9935-4E4BBFA7D88DQ24814780-5B321078-A4DB-4B68-BA4D-EA26924086A7Q27621369-CE29B0C7-A817-4D96-9406-8AD1FAC975FFQ27625877-C29F151D-8F1E-4EEB-B853-45B6D95D90F4Q27637348-F5A5EEA7-626A-4F7B-8870-D6C409A68FE0Q27640283-57027B89-1AE9-4E91-ABF7-AD2636374D8FQ27641284-A78ECE89-0A8D-487B-96D0-53FFDD7271C9Q27641515-6540FDAA-2A50-40E9-A5E2-E06901C3227EQ27641612-F5D09BF8-315C-4C8A-9DB0-DE56902E4784Q27641734-276A2436-969D-4A5F-A621-BB603A2BA4EFQ27644214-64BD021E-F4A3-4E45-B7B7-C21C86EC2FF4Q27644275-F77C3B7D-D4E5-4933-BB56-3D686EB331C4Q27648365-B22236C0-8D25-4D49-A9A8-B2138C747DB4Q27649910-CAE1B92F-39F5-4362-9187-52BDFC28A749Q27650725-29731544-1A0A-4B8B-9E78-2A60DC723000Q27652096-903825A2-D4A1-4FD4-AFF1-43EB8C97D930Q27653590-86511A7B-FE01-4A6A-AB50-1BE019184680Q27653918-CD96D993-082E-4CA4-861A-B6FB3D7AFA6EQ27657064-CF468016-DEDF-4C5E-A724-0EBF53690F76Q27658016-389457E3-6CAF-4DBA-AD39-205A230D7903Q27658834-F3ADF9B7-B939-4ADB-A375-E6B991BE4DF7Q27663644-DE0282D6-4CA4-4D3D-BE35-3C2388B41A1BQ27664676-1E4FEF27-C9DC-43A2-A820-5660A578E382Q27664730-292CCEEE-06E3-438B-95FF-595EF451B78FQ27665746-143DA646-A1F3-44FB-8DAE-49C726908839Q27665931-A10A97BB-7E06-4606-96FE-D1404212B3BAQ27673356-B9565BE8-C3BC-47CE-80D2-6A936D88B486Q27674692-E913983D-A71C-49F7-B796-952596A2A8DAQ27675630-7629B33F-551C-45D1-9691-6504A68EB247Q27676672-BB84A24C-A04F-4573-8397-7A9609FA8378Q27677724-E2178846-6BA3-4642-99B0-9FD3ADCFCF51Q27679398-EFC8F20A-F899-4C2A-80AE-6087924CE4EDQ27679409-1A3D3ECA-B59C-4BB2-9AA6-00044AE1F51CQ27680775-FB0ADE6B-FC6D-4683-8E4B-8F510F3ABB49Q27681308-00ED1364-96D1-42F4-A842-ADA95D4F3343Q27681446-0AD3E4FB-DD82-4EE1-908E-A9C805FA7461Q27681710-2888C20E-B2CE-4543-A403-69297706A8A0
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Todd O Yeates
@nl
Todd O Yeates
@sl
Todd O. Yeates
@en
Todd O. Yeates
@es
type
label
Todd O Yeates
@nl
Todd O Yeates
@sl
Todd O. Yeates
@en
Todd O. Yeates
@es
altLabel
Todd Yeates
@en
Yeates TO
@en
prefLabel
Todd O Yeates
@nl
Todd O Yeates
@sl
Todd O. Yeates
@en
Todd O. Yeates
@es
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7005184258
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vuAMQKYAAAAJ
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0000-0001-5709-9839