3IXV
 
 | | Scorpion Hemocyanin resting state pseudo atomic model built based on cryo-EM density map | | Descriptor: | Hemocyanin AA6 chain | | Authors: | Cong, Y, Zhang, Q, Woolford, D, Schweikardt, T, Khant, H, Ludtke, S, Chiu, W, Decker, H. | | Deposit date: | 2009-02-13 | | Release date: | 2009-06-02 | | Last modified: | 2024-02-21 | | Method: | ELECTRON MICROSCOPY (6.8 Å) | | Cite: | Structural Mechanism of SDS-Induced Enzyme Activity of Scorpion Hemocyanin Revealed by Electron Cryomicroscopy.
Structure, 17, 2009
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3IXW
 | | Scorpion Hemocyanin activated state pseudo atomic model built based on cryo-EM density map | | Descriptor: | Hemocyanin AA6 chain | | Authors: | Cong, Y, Zhang, Q, Woolford, D, Schweikardt, T, Khant, H, Ludtke, S, Chiu, W, Decker, H. | | Deposit date: | 2009-02-13 | | Release date: | 2009-06-02 | | Last modified: | 2024-02-21 | | Method: | ELECTRON MICROSCOPY (8 Å) | | Cite: | Structural Mechanism of SDS-Induced Enzyme Activity of Scorpion Hemocyanin Revealed by Electron Cryomicroscopy.
Structure, 17, 2009
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3KTT
 | | Atomic model of bovine TRiC CCT2(beta) subunit derived from a 4.0 Angstrom cryo-EM map | | Descriptor: | T-complex protein 1 subunit beta | | Authors: | Cong, Y, Baker, M.L, Ludtke, S.J, Frydman, J, Chiu, W. | | Deposit date: | 2009-11-25 | | Release date: | 2010-03-16 | | Last modified: | 2024-02-21 | | Method: | ELECTRON MICROSCOPY (4 Å) | | Cite: | 4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
Proc.Natl.Acad.Sci.USA, 107, 2010
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3IYG
 | | Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map | | Descriptor: | T-complex protein 1 subunit, T-complex protein 1 subunit alpha, T-complex protein 1 subunit beta, ... | | Authors: | Cong, Y, Baker, M.L, Ludtke, S.J, Frydman, J, Chiu, W. | | Deposit date: | 2009-11-28 | | Release date: | 2010-03-16 | | Last modified: | 2024-02-21 | | Method: | ELECTRON MICROSCOPY (4 Å) | | Cite: | 4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
Proc.Natl.Acad.Sci.USA, 107, 2010
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