1C6J
 
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1C6K
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1C6M
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1C6L
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1C66
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1C6N
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1C6A
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177L
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176L
 | | PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME | | Descriptor: | CHLORIDE ION, T4 LYSOZYME | | Authors: | Zhang, X.-J, Weaver, L, Dubose, R, Matthews, B.W. | | Deposit date: | 1995-03-24 | | Release date: | 1995-07-10 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.
J.Mol.Biol., 250, 1995
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180L
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178L
 | | Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME | | Descriptor: | CHLORIDE ION, T4 LYSOZYME | | Authors: | Matsumura, M, Weaver, L, Zhang, X.-J, Matthews, B.W. | | Deposit date: | 1995-03-24 | | Release date: | 1995-07-10 | | Last modified: | 2021-11-03 | | Method: | X-RAY DIFFRACTION (2.71 Å) | | Cite: | Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.
J.Mol.Biol., 250, 1995
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1NHB
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1P5C
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1P56
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1QSQ
 | | CAVITY CREATING MUTATION | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J, Matthews, B.W. | | Deposit date: | 1999-06-22 | | Release date: | 1999-06-29 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.9 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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1CV1
 | | T4 LYSOZYME MUTANT V111M | | 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: | 1999-11-10 | | 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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1CV5
 | | T4 LYSOZYME MUTANT L133M | | 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: | 1999-11-10 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (1.87 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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1D3F
 | | N-TERMINAL DOMAIN CORE METHIONINE MUTATION | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Matthews, B.W. | | Deposit date: | 1999-09-29 | | Release date: | 1999-10-08 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.05 Å) | | Cite: | Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
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1D3M
 | | METHIONINE CORE MUTATION | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Matthews, B.W. | | Deposit date: | 1999-09-29 | | Release date: | 1999-09-30 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.12 Å) | | Cite: | Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
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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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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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1CU0
 | | T4 LYSOZYME MUTANT I78M | | 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: | 1999-11-10 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.2 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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1CV4
 | | T4 LYSOZYME MUTANT L118M | | 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: | 1999-11-10 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (1.9 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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1CVK
 | | T4 LYSOZYME MUTANT L118A | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | Deposit date: | 1999-08-23 | | Release date: | 1999-11-10 | | 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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