6JNA
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![BU of 6jna by Molmil](/molmil-images/mine/6jna) | Cryo-EM structure of glutamate dehydrogenase from Thermococcus profundus | 分子名称: | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, Glutamate dehydrogenase | 著者 | Oide, M, Kato, T, Oroguchi, T, Nakasako, M. | 登録日 | 2019-03-14 | 公開日 | 2020-02-12 | 最終更新日 | 2024-03-27 | 実験手法 | ELECTRON MICROSCOPY (3.8 Å) | 主引用文献 | Energy landscape of domain motion in glutamate dehydrogenase deduced from cryo-electron microscopy. Febs J., 287, 2020
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6JN9
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![BU of 6jn9 by Molmil](/molmil-images/mine/6jn9) | Cryo-EM structure of glutamate dehydrogenase from Thermococcus profundus | 分子名称: | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, Glutamate dehydrogenase | 著者 | Oide, M, Kato, T, Oroguchi, T, Nakasako, M. | 登録日 | 2019-03-14 | 公開日 | 2020-02-12 | 最終更新日 | 2024-03-27 | 実験手法 | ELECTRON MICROSCOPY (3.8 Å) | 主引用文献 | Energy landscape of domain motion in glutamate dehydrogenase deduced from cryo-electron microscopy. Febs J., 287, 2020
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6JNC
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![BU of 6jnc by Molmil](/molmil-images/mine/6jnc) | Cryo-EM structure of glutamate dehydrogenase from Thermococcus profundus | 分子名称: | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, Glutamate dehydrogenase | 著者 | Oide, M, Kato, T, Oroguchi, T, Nakasako, M. | 登録日 | 2019-03-14 | 公開日 | 2020-02-12 | 最終更新日 | 2024-03-27 | 実験手法 | ELECTRON MICROSCOPY (3.7 Å) | 主引用文献 | Energy landscape of domain motion in glutamate dehydrogenase deduced from cryo-electron microscopy. Febs J., 287, 2020
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6JND
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![BU of 6jnd by Molmil](/molmil-images/mine/6jnd) | Cryo-EM structure of glutamate dehydrogenase from Thermococcus profundus | 分子名称: | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, Glutamate dehydrogenase | 著者 | Oide, M, Kato, T, Oroguchi, T, Nakasako, M. | 登録日 | 2019-03-14 | 公開日 | 2020-02-12 | 最終更新日 | 2024-03-27 | 実験手法 | ELECTRON MICROSCOPY (3.9 Å) | 主引用文献 | Energy landscape of domain motion in glutamate dehydrogenase deduced from cryo-electron microscopy. Febs J., 287, 2020
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2RQ7
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![BU of 2rq7 by Molmil](/molmil-images/mine/2rq7) | Solution structure of the epsilon subunit chimera combining the N-terminal beta-sandwich domain from T. Elongatus bp-1 f1 and the C-terminal alpha-helical domain from spinach chloroplast F1 | 分子名称: | ATP synthase epsilon chain,ATP synthase epsilon chain, chloroplastic | 著者 | Yagi, H, Konno, H, Murakami-Fuse, T, Oroguchi, H, Akutsu, T, Ikeguchi, M, Hisabori, T. | 登録日 | 2009-03-03 | 公開日 | 2010-01-12 | 最終更新日 | 2024-05-01 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural and functional analysis of the intrinsic inhibitor subunit epsilon of F1-ATPase from photosynthetic organisms. Biochem.J., 425, 2010
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2RQ6
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![BU of 2rq6 by Molmil](/molmil-images/mine/2rq6) | Solution structure of the epsilon subunit of the F1-atpase from thermosynechococcus elongatus BP-1 | 分子名称: | ATP synthase epsilon chain | 著者 | Yagi, H, Konno, H, Murakami-Fuse, T, Oroguchi, H, Akutsu, T, Ikeguchi, M, Hisabori, T. | 登録日 | 2009-03-03 | 公開日 | 2010-01-12 | 最終更新日 | 2024-05-29 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural and functional analysis of the intrinsic inhibitor subunit epsilon of F1-ATPase from photosynthetic organisms. Biochem.J., 425, 2010
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6S58
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![BU of 6s58 by Molmil](/molmil-images/mine/6s58) | AvaII restriction endonuclease in the absence of nucleic acids | 分子名称: | CALCIUM ION, Type II site-specific deoxyribonuclease, UNKNOWN ATOM OR ION | 著者 | Kisiala, M, Kowalska, M, Korza, H, Czapinska, H, Bochtler, M. | 登録日 | 2019-06-30 | 公開日 | 2020-05-20 | 最終更新日 | 2024-01-24 | 実験手法 | X-RAY DIFFRACTION (2.32 Å) | 主引用文献 | Restriction endonucleases that cleave RNA/DNA heteroduplexes bind dsDNA in A-like conformation. Nucleic Acids Res., 48, 2020
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6S48
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![BU of 6s48 by Molmil](/molmil-images/mine/6s48) | AvaII RESTRICTION ENDONUCLEASE IN COMPLEX WITH PARTIALLY CLEAVED dsDNA | 分子名称: | BETA-MERCAPTOETHANOL, CALCIUM ION, DNA (5'-D(*GP*AP*TP*G)-3'), ... | 著者 | Kisiala, M, Kowalska, M, Korza, H, Czapinska, H, Bochtler, M. | 登録日 | 2019-06-26 | 公開日 | 2020-05-20 | 最終更新日 | 2024-01-24 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | Restriction endonucleases that cleave RNA/DNA heteroduplexes bind dsDNA in A-like conformation. Nucleic Acids Res., 48, 2020
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