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Showing all 34 items for (author: stillman & b)

EMDB-23755:
CryoEM map of the structure of the S. cerevisiae origin recognition complex bound to the replication initiator Cdc6 and the ARS1 origin DNA.
Method: single particle / : Feng X, Li H

EMDB-23818:
Cryo-EM 3D map of the S. cerevisiae origin recognition complex bound to Cdc6 and ARS1 origin DNA
Method: single particle / : Feng X, Li H

PDB-7mca:
Structure of the S. cerevisiae origin recognition complex bound to the replication initiator Cdc6 and the ARS1 origin DNA.
Method: single particle / : Feng X, Li H

EMDB-22418:
ORC-O2WH: Human Origin Recognition Complex (ORC) with dynamic/unresolved ORC1 AAA+ domain
Method: single particle / : Jaremko MJ, Joshua-Tor L

EMDB-22420:
ORC-OPEN: Human Origin Recognition Complex (ORC) in an open conformation
Method: single particle / : Jaremko MJ, Joshua-Tor L

EMDB-22421:
ORC-DNA: Human Origin Recognition Complex (ORC) with DNA bound in the core
Method: single particle / : Jaremko MJ, Joshua-Tor L

PDB-7jpp:
ORC-O2WH: Human Origin Recognition Complex (ORC) with dynamic/unresolved ORC1 AAA+ domain
Method: single particle / : Jaremko MJ, Joshua-Tor L

PDB-7jpr:
ORC-OPEN: Human Origin Recognition Complex (ORC) in an open conformation
Method: single particle / : Jaremko MJ, Joshua-Tor L

PDB-7jps:
ORC-DNA: Human Origin Recognition Complex (ORC) with DNA bound in the core
Method: single particle / : Jaremko MJ, Joshua-Tor L

EMDB-22417:
ORC-O1AAA: Human Origin Recognition Complex (ORC) with dynamic/unresolved ORC2 WH
Method: single particle / : Jaremko MJ, Joshua-Tor L

EMDB-22419:
ORC-O2-5: Human Origin Recognition Complex (ORC) with subunits 2,3,4,5
Method: single particle / : Jaremko MJ, Joshua-Tor L

PDB-7jpo:
ORC-O1AAA: Human Origin Recognition Complex (ORC) with dynamic/unresolved ORC2 WH
Method: single particle / : Jaremko MJ, Joshua-Tor L

PDB-7jpq:
ORC-O2-5: Human Origin Recognition Complex (ORC) with subunits 2,3,4,5
Method: single particle / : Jaremko MJ, Joshua-Tor L

EMDB-21662:
Cryo-EM map of semi-attached mutant OCCM-DNA complex (ORC-Cdc6-Cdt1-Mcm2-7 with Mcm6 WHD truncation)
Method: single particle / : Yuan Z, Schneider S

EMDB-21664:
Cryo-EM map of mutant Mcm2-7 hexamer with Mcm6 WHD truncation
Method: single particle / : Yuan Z, Schneider S

EMDB-21665:
Cryo-EM map of pre-insertion mutant OCCM-DNA complex (ORC-Cdc6-Cdt1-Mcm2-7 with Mcm6 WHD truncation)
Method: single particle / : Yuan Z, Schneider S

EMDB-21666:
Cryo-EM map of the mutant OCCM (ORC-Cdc6-Cdt1-Mcm2-7 with Mcm6 WHD truncation) loaded on DNA at 10.5 A resolution
Method: single particle / : Yuan Z, Schneider S

PDB-6wgc:
Atomic model of semi-attached mutant OCCM-DNA complex (ORC-Cdc6-Cdt1-Mcm2-7 with Mcm6 WHD truncation)
Method: single particle / : Yuan Z, Schneider S, Dodd T, Riera A, Bai L, Yan C, Magdalou I, Ivanov I, Stillman B, Li H, Speck C

PDB-6wgf:
Atomic model of mutant Mcm2-7 hexamer with Mcm6 WHD truncation
Method: single particle / : Yuan Z, Schneider S, Dodd T, Riera A, Bai L, Yan C, Magdalou I, Ivanov I, Stillman B, Li H, Speck C

PDB-6wgg:
Atomic model of pre-insertion mutant OCCM-DNA complex(ORC-Cdc6-Cdt1-Mcm2-7 with Mcm6 WHD truncation)
Method: single particle / : Yuan Z, Schneider S, Dodd T, Riera A, Bai L, Yan C, Magdalou I, Ivanov I, Stillman B, Li H, Speck C

PDB-6wgi:
Atomic model of the mutant OCCM (ORC-Cdc6-Cdt1-Mcm2-7 with Mcm6 WHD truncation) loaded on DNA at 10.5 A resolution
Method: single particle / : Yuan Z, Schneider S, Dodd T, Riera A, Bai L, Yan C, Magdalou I, Ivanov I, Stillman B, Li H, Speck C

EMDB-8523:
Structure of the active form of human Origin Recognition Complex and its ATPase motor module
Method: single particle / : Sun J, Li H

EMDB-9400:
Cryo-EM structure of Mcm2-7 double hexamer on dsDNA
Method: single particle / : Li H, Yuan Z, Bai L

PDB-5bk4:
Cryo-EM structure of Mcm2-7 double hexamer on dsDNA
Method: single particle / : Li H, Yuan Z, Bai L

PDB-5v8f:
Structural basis of MCM2-7 replicative helicase loading by ORC-Cdc6 and Cdt1
Method: single particle / : Yuan Z, Riera A, Bai L, Sun J, Spanos C, Chen ZA, Barbon M, Rappsilber J, Stillman B, Speck C, Li H

EMDB-8540:
Structural basis of MCM2-7 replicative helicase loading by ORC-Cdc6 and Cdt1
Method: single particle / : Yuan Z, Riera A, Bai L, Sun J, Spanos C, Chen ZA, Barbon M, Rappsilber J, Stillman B, Speck C, Li H

EMDB-8541:
Structure of the active form of human Origin Recognition Complex and its ATPase motor module
Method: single particle / : Tocilj A, On K, Yuan Z, Sun J, Elkayam E, Li H, Stillman B, Joshua-Tor L

PDB-5ujm:
Structure of the active form of human Origin Recognition Complex and its ATPase motor module
Method: single particle / : Tocilj A, On K, Yuan Z, Sun J, Elkayam E, Li H, Stillman B, Joshua-Tor L

EMDB-5857:
Architectures of Mcm2-7 Double Hexamer Assembly Intermediates Reveal Helicase Loading Mechanism
Method: single particle / : Sun J, Fernandez-Cid A, Riera A, Stillman B, Speck C, Li H

EMDB-5625:
Architecture of a helicase loading intermediate containing ORC-Cdc6-Cdt1-MCM2-7 on DNA reveals similarity to DNA polymerase clamp loading complexes
Method: single particle / : Sun J, Evrin C, Samel S, Fernandez-Cid A, Riera A, Kawakami H, Stillman B, Speck C, Li H

EMDB-5381:
Cdc6-induced Conformational Changes in ORC Bound To Origin DNA Revealed by Cryo-Electron Microscopy. This map may be mirrored (based on comparison to EMD-5625).
Method: single particle / : Sun J, Kawakami H, Zech J, Speck C, Stillman B, Li H

EMDB-5013:
A 3D EM map of the subcomplex Orc1-5 of the yeast origin recognition complex (ORC).
Method: single particle / : Chen Z, Speck C, Wendel P, Tang C, Stillman B, Li H

EMDB-1156:
ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA.
Method: single particle / : Speck C, Chen Z, Li H, Stillman B

EMDB-1157:
ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA.
Method: single particle / : Speck C, Chen Z, Li H, Stillman B

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Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

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Oct 5, 2021. Nobel Prize for mechanically activated and temperature-gated ion channels

Nobel Prize for mechanically activated and temperature-gated ion channels

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