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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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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1D2Y
 | | N-TERMINAL DOMAIN CORE METHIONINE MUTATION | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Matthews, B.W. | | Deposit date: | 1999-09-28 | | Release date: | 1999-10-08 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.06 Å) | | Cite: | Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
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1D2W
 | | N-TERMINAL DOMAIN CORE METHIONINE MUTATION | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Matthews, B.W. | | Deposit date: | 1999-09-28 | | Release date: | 1999-10-08 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (1.89 Å) | | Cite: | Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
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1D3J
 | | 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 (1.97 Å) | | Cite: | Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
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1D3N
 | | 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: | 2021-11-03 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
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1KW7
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | Deposit date: | 2002-01-28 | | Release date: | 2003-06-03 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.89 Å) | | Cite: | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
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1KS3
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | Deposit date: | 2002-01-10 | | Release date: | 2003-06-03 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.16 Å) | | Cite: | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
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1KW5
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | Deposit date: | 2002-01-28 | | Release date: | 2003-06-03 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.75 Å) | | Cite: | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
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1KY0
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | Deposit date: | 2002-02-01 | | Release date: | 2003-06-03 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.97 Å) | | Cite: | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
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1KY1
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | Deposit date: | 2002-02-01 | | Release date: | 2003-06-03 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.05 Å) | | Cite: | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
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1L0K
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | Deposit date: | 2002-02-11 | | Release date: | 2003-06-03 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.02 Å) | | Cite: | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
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1L0J
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | Authors: | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | Deposit date: | 2002-02-11 | | Release date: | 2003-06-03 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.98 Å) | | Cite: | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
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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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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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1CU2
 | | T4 LYSOZYME MUTANT L84M | | 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 (1.85 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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1CUQ
 | | T4 LYSOZYME MUTANT V103M | | 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 (2.05 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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1CV0
 | | T4 LYSOZYME MUTANT F104M | | 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 (2.12 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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1CU5
 | | T4 LYSOZYME MUTANT L91M | | 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: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.05 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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1CV6
 | | T4 LYSOZYME MUTANT V149M | | 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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