2BO1
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1W41
| T. celer L30e E90A variant | Descriptor: | 50S RIBOSOMAL PROTEIN L30E | Authors: | Lee, C.F, Lee, K.M, Chan, S.H, Allen, M.D, Bycroft, M, Wong, K.B. | Deposit date: | 2004-07-22 | Release date: | 2005-04-08 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Electrostatic Interactions Contribute to Reduced Heat Capacity Change of Unfolding in a Thermophilic Ribosomal Protein L30E J.Mol.Biol., 348, 2005
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1W42
| T. celer L30e R92A variant | Descriptor: | 50S RIBOSOMAL PROTEIN L30E | Authors: | Lee, C.F, Lee, K.M, Chan, S.H, Allen, M.D, Bycroft, M, Wong, K.B. | Deposit date: | 2004-07-22 | Release date: | 2005-04-08 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Electrostatic Interactions Contribute to Reduced Heat Capacity Change of Unfolding in a Thermophilic Ribosomal Protein L30E J.Mol.Biol., 348, 2005
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1W40
| T. celer L30e K9A variant | Descriptor: | 50S RIBOSOMAL PROTEIN L30E | Authors: | Lee, C.F, Lee, K.M, Chan, S.H, Allen, M.D, Bycroft, M, Wong, K.B. | Deposit date: | 2004-07-22 | Release date: | 2005-04-08 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.03 Å) | Cite: | Electrostatic Interactions Contribute to Reduced Heat Capacity Change of Unfolding in a Thermophilic Ribosomal Protein L30E J.Mol.Biol., 348, 2005
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3NOW
| UNC-45 from Drosophila melanogaster | Descriptor: | UNC-45 protein, SD10334p | Authors: | Lee, C.F, Hauenstein, A.V, Fleming, J.K, Gasper, W.C, Engelke, V, Banumathi, S, Bernstein, S.I, Huxford, T. | Deposit date: | 2010-06-25 | Release date: | 2011-03-16 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (2.992 Å) | Cite: | X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster. Structure, 19, 2011
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1W3E
| Ribosomal L30e of Thermococcus celer, P59A mutant | Descriptor: | 50S RIBOSOMAL PROTEIN L30E | Authors: | Ma, H.W, Lee, C.F, Allen, M.D, Bycroft, M, Wong, K.B. | Deposit date: | 2004-07-15 | Release date: | 2006-10-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.77 Å) | Cite: | Role of Proline Residues in Thermostability of T. Celer L30E Protein To be Published
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