4CI0
| Electron cryo-microscopy of F420-reducing NiFe hydrogenase Frh | Descriptor: | F420-REDUCING HYDROGENASE, SUBUNIT ALPHA, SUBUNIT BETA, ... | Authors: | Allegretti, M, Mills, D.J, McMullan, G, Kuehlbrandt, W, Vonck, J. | Deposit date: | 2013-12-05 | Release date: | 2014-02-26 | Last modified: | 2019-11-20 | Method: | ELECTRON MICROSCOPY (3.36 Å) | Cite: | Atomic Model of the F420-Reducing [Nife] Hydrogenase by Electron Cryo-Electron Microscopy Using a Direct Electron Detector. Elife, 3, 2014
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6YVV
| Condensin complex from S.cerevisiae ATP-free apo bridged state | Descriptor: | Condensin complex subunit 1,Ycs4, Condensin complex subunit 2,Brn1, Structural maintenance of chromosomes protein 2,Structural maintenance of chromosomes protein 2, ... | Authors: | Lee, B.-G, Cawood, C, Gutierrez-Escribano, P, Nakane, T, Merkel, F, Hassler, M, Haering, C.H, Aragon, L, Lowe, J. | Deposit date: | 2020-04-28 | Release date: | 2020-07-15 | Last modified: | 2024-05-22 | Method: | ELECTRON MICROSCOPY (7.5 Å) | Cite: | Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism. Nat.Struct.Mol.Biol., 27, 2020
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6YVD
| Head segment of the S.cerevisiae condensin holocomplex in presence of ATP | Descriptor: | Condensin complex subunit 2, Condensin complex subunit 3, Structural maintenance of chromosomes protein 2, ... | Authors: | Merkel, F, Haering, C.H, Hassler, M, Lee, B.G, Lowe, J. | Deposit date: | 2020-04-28 | Release date: | 2020-07-22 | Last modified: | 2024-07-10 | Method: | ELECTRON MICROSCOPY (7.6 Å) | Cite: | Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism. Nat.Struct.Mol.Biol., 27, 2020
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6YVU
| Condensin complex from S.cerevisiae ATP-free apo non-engaged state | Descriptor: | Condensin complex subunit 1,Condensin complex subunit 1,Ycs4, Condensin complex subunit 2,Condensin complex subunit 2,Brn1, Structural maintenance of chromosomes protein 2,Structural maintenance of chromosomes protein 2,Smc2, ... | Authors: | Lee, B.-G, Cawood, C, Gutierrez-Escribano, P, Nakane, T, Merkel, F, Hassler, M, Aragon, L, Haering, C.H, Lowe, J. | Deposit date: | 2020-04-28 | Release date: | 2020-07-15 | Last modified: | 2024-05-22 | Method: | ELECTRON MICROSCOPY (7.5 Å) | Cite: | Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism. Nat.Struct.Mol.Biol., 27, 2020
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7TBI
| Composite structure of the S. cerevisiae nuclear pore complex (NPC) | Descriptor: | Dyn2, Nic96 R1, Nic96 R2, ... | Authors: | Petrovic, S, Samanta, D, Perriches, T, Bley, C.J, Thierbach, K, Brown, B, Nie, S, Mobbs, G.W, Stevens, T.A, Liu, X, Tomaleri, G.P, Schaus, L, Hoelz, A. | Deposit date: | 2021-12-22 | Release date: | 2022-06-15 | Last modified: | 2024-10-16 | Method: | ELECTRON MICROSCOPY (25 Å) | Cite: | Architecture of the linker-scaffold in the nuclear pore. Science, 376, 2022
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7TBM
| Composite structure of the dilated human nuclear pore complex (NPC) generated with a 37A in situ cryo-ET map of CD4+ T cell NPC | Descriptor: | DDX19, NUP107 CTD, NUP107 NTD, ... | Authors: | Bley, C.J, Nie, S, Mobbs, G.W, Petrovic, S, Gres, A.T, Liu, X, Mukherjee, S, Harvey, S, Huber, F.M, Lin, D.H, Brown, B, Tang, A.W, Rundlet, E.J, Correia, A.R, Chen, S, Regmi, S.G, Stevens, T.A, Jette, C.A, Dasso, M, Patke, A, Palazzo, A.F, Kossiakoff, A.A, Hoelz, A. | Deposit date: | 2021-12-22 | Release date: | 2022-06-15 | Last modified: | 2022-06-22 | Method: | ELECTRON MICROSCOPY (37 Å) | Cite: | Architecture of the cytoplasmic face of the nuclear pore. Science, 376, 2022
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7TBK
| Composite structure of the dilated human nuclear pore complex (NPC) symmetric core generated with a 37A in situ cryo-ET map of CD4+ T cell NPC | Descriptor: | NUP107 CTD, NUP107 NTD, NUP133, ... | Authors: | Petrovic, S, Samanta, D, Perriches, T, Bley, C.J, Thierbach, K, Brown, B, Nie, S, Mobbs, G.W, Stevens, T.A, Liu, X, Tomaleri, G.P, Schaus, L, Hoelz, A. | Deposit date: | 2021-12-22 | Release date: | 2022-06-15 | Last modified: | 2022-06-22 | Method: | ELECTRON MICROSCOPY (37 Å) | Cite: | Architecture of the linker-scaffold in the nuclear pore. Science, 376, 2022
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