1QSQ
 
 | | CAVITY CREATING MUTATION | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Matthews, B.W. | | 登録日 | 1999-06-22 | | 公開日 | 1999-06-29 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | 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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1CTW
 | | T4 LYSOZYME MUTANT I78A | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | 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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1CU6
 | | T4 LYSOZYME MUTANT L91A | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-17 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | 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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1CU0
 | | T4 LYSOZYME MUTANT I78M | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.2 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-22 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-23 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.05 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.12 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (2.05 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-22 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | 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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1CU3
 | | T4 LYSOZYME MUTANT V87M | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.12 Å) | | 主引用文献 | 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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1CUP
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.89 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-20 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-22 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.87 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-22 | | 公開日 | 1999-08-24 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Lindstrom, J, Lu, J, Matthews, B.W. | | 登録日 | 1999-08-28 | | 公開日 | 1999-11-10 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.94 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | 登録日 | 2002-01-28 | | 公開日 | 2003-06-03 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.89 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | 登録日 | 2002-01-10 | | 公開日 | 2003-06-03 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (2.16 Å) | | 主引用文献 | 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 | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | 登録日 | 2002-01-28 | | 公開日 | 2003-06-03 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.75 Å) | | 主引用文献 | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
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1D2Y
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1D2W
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1D3J
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1D3N
 | | METHIONINE CORE MUTATION | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Matthews, B.W. | | 登録日 | 1999-09-29 | | 公開日 | 1999-09-30 | | 最終更新日 | 2024-10-30 | | 実験手法 | X-RAY DIFFRACTION (2 Å) | | 主引用文献 | Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr.,Sect.D, 55, 1999
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1KY0
 | | METHIONINE CORE MUTANT OF T4 LYSOZYME | | 分子名称: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | | 著者 | Gassner, N.C, Baase, W.A, Mooers, B.H, Busam, R.D, Weaver, L.H, Lindstrom, J.D, Quillin, M.L, Matthews, B.W. | | 登録日 | 2002-02-01 | | 公開日 | 2003-06-03 | | 最終更新日 | 2024-02-14 | | 実験手法 | X-RAY DIFFRACTION (1.97 Å) | | 主引用文献 | Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability
BIOPHYS.CHEM., 100, 2003
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