1L09
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1L26
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1L44
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1L58
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1CX7
| T4 LYSOZYME METHIONINE CORE MUTANT | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-28 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.94 Å) | Cite: | Use of differentially substituted selenomethionine proteins in X-ray structure determination. Acta Crystallogr.,Sect.D, 55, 1999
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1L64
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1L71
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1L76
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1L91
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1L96
| STRUCTURE OF A HINGE-BENDING BACTERIOPHAGE T4 LYSOZYME MUTANT, ILE3-> PRO | Descriptor: | BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME | Authors: | Dixon, M, Shewchuk, L, Matthews, B.W. | Deposit date: | 1992-02-11 | Release date: | 1993-10-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3-->Pro. J.Mol.Biol., 227, 1992
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1LGW
| T4 Lysozyme Mutant L99A/M102Q Bound by 2-fluoroaniline | Descriptor: | 2-FLUOROANILINE, BETA-MERCAPTOETHANOL, CHLORIDE ION, ... | Authors: | Wei, B.Q, Baase, W.A, Weaver, L.H, Matthews, B.W, Shoichet, B.K. | Deposit date: | 2002-04-16 | Release date: | 2002-05-08 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | A Model Binding Site for Testing Scoring Functions in Molecular Docking J.Mol.Biol., 322, 2002
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1L87
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1CU6
| T4 LYSOZYME MUTANT L91A | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-20 | Release date: | 1999-11-17 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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1CV3
| T4 LYSOZYME MUTANT L121M | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-22 | Release date: | 1999-08-24 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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1L30
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1L36
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1L63
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1L52
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1L80
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1L89
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1L77
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1L92
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1L97
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1C6N
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1C66
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