2IOS
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3OII
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3O7B
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3OIJ
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3OIN
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6U18
| Directed evolution of a biosensor selective for the macrolide antibiotic clarithromycin | 分子名称: | CITRATE ANION, CLARITHROMYCIN, Erythromycin resistance repressor protein | 著者 | Li, Y, Reed, M, Wright, H.T, Cropp, T.A, Williams, G. | 登録日 | 2019-08-15 | 公開日 | 2020-08-19 | 最終更新日 | 2023-10-11 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | Development of Genetically Encoded Biosensors for Reporting the Methyltransferase-Dependent Biosynthesis of Semisynthetic Macrolide Antibiotics. Acs Synth Biol, 2021
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4PKN
| Crystal structure of the football-shaped GroEL-GroES2-(ADPBeFx)14 complex containing substrate Rubisco | 分子名称: | 10 kDa chaperonin, 60 kDa chaperonin, ADENOSINE-5'-DIPHOSPHATE, ... | 著者 | Fei, X, Ye, X, Laronde-Leblanc, N, Lorimer, G.H. | 登録日 | 2014-05-15 | 公開日 | 2014-08-20 | 最終更新日 | 2023-12-27 | 実験手法 | X-RAY DIFFRACTION (3.66 Å) | 主引用文献 | Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form. Proc.Natl.Acad.Sci.USA, 111, 2014
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4PKO
| Crystal structure of the Football-shaped GroEL-GroES2-(ADPBeFx)14 complex | 分子名称: | 10 kDa chaperonin, 60 kDa chaperonin, ADENOSINE-5'-DIPHOSPHATE, ... | 著者 | Fei, X, Ye, X, Laronde-Leblanc, N, Lorimer, G.H. | 登録日 | 2014-05-15 | 公開日 | 2014-08-20 | 最終更新日 | 2023-12-27 | 実験手法 | X-RAY DIFFRACTION (3.84 Å) | 主引用文献 | Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form. Proc.Natl.Acad.Sci.USA, 111, 2014
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1Z0W
| Crystal Structure of A. fulgidus Lon proteolytic domain at 1.2A resolution | 分子名称: | CALCIUM ION, Putative protease La homolog type | 著者 | Botos, I, Melnikov, E.E, Cherry, S, Kozlov, S, Makhovskaya, O.V, Tropea, J.E, Gustchina, A, Rotanova, T.V, Wlodawer, A. | 登録日 | 2005-03-02 | 公開日 | 2005-08-02 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.2 Å) | 主引用文献 | Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases J.Mol.Biol., 351, 2005
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1Z0B
| Crystal Structure of A. fulgidus Lon proteolytic domain E506A mutant | 分子名称: | CALCIUM ION, Putative protease La homolog type | 著者 | Botos, I, Melnikov, E.E, Cherry, S, Kozlov, S, Makhovskaya, O.V, Tropea, J.E, Gustchina, A, Rotanova, T.V, Wlodawer, A. | 登録日 | 2005-03-01 | 公開日 | 2005-08-02 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.55 Å) | 主引用文献 | Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases J.Mol.Biol., 351, 2005
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1Z0E
| Crystal Structure of A. fulgidus Lon proteolytic domain | 分子名称: | Putative protease La homolog type | 著者 | Botos, I, Melnikov, E.E, Cherry, S, Kozlov, S, Makhovskaya, O.V, Tropea, J.E, Gustchina, A, Rotanova, T.V, Wlodawer, A. | 登録日 | 2005-03-01 | 公開日 | 2005-08-02 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2.05 Å) | 主引用文献 | Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases J.Mol.Biol., 351, 2005
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1Z0C
| Crystal Structure of A. fulgidus Lon proteolytic domain D508A mutant | 分子名称: | Putative protease La homolog type | 著者 | Botos, I, Melnikov, E.E, Cherry, S, Kozlov, S, Makhovskaya, O.V, Tropea, J.E, Gustchina, A, Rotanova, T.V, Wlodawer, A. | 登録日 | 2005-03-01 | 公開日 | 2005-08-02 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.55 Å) | 主引用文献 | Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases J.Mol.Biol., 351, 2005
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1Z0G
| Crystal Structure of A. fulgidus Lon proteolytic domain | 分子名称: | Putative protease La homolog type | 著者 | Botos, I, Melnikov, E.E, Cherry, S, Kozlov, S, Makhovskaya, O.V, Tropea, J.E, Gustchina, A, Rotanova, T.V, Wlodawer, A. | 登録日 | 2005-03-01 | 公開日 | 2005-08-02 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2.27 Å) | 主引用文献 | Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases J.Mol.Biol., 351, 2005
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