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1CV3
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BU of 1cv3 by Molmil
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
1CX7
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BU of 1cx7 by Molmil
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
1CU0
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BU of 1cu0 by Molmil
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
1CV4
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BU of 1cv4 by Molmil
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
1CU2
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BU of 1cu2 by Molmil
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
1CUQ
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BU of 1cuq by Molmil
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
1CV0
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BU of 1cv0 by Molmil
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
1CTW
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BU of 1ctw by Molmil
T4 LYSOZYME MUTANT I78A
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
1CU5
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BU of 1cu5 by Molmil
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
1CV6
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BU of 1cv6 by Molmil
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
1CX6
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BU of 1cx6 by Molmil
T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE
Descriptor: 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME
Authors:Gassner, N.C, Baase, W.A, Matthews, B.W.
Deposit date:1999-08-28
Release date:1999-12-15
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.01 Å)
Cite:Substitution with selenomethionine can enhance the stability of methionine-rich proteins.
J.Mol.Biol., 294, 1999
1CU3
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BU of 1cu3 by Molmil
T4 LYSOZYME MUTANT V87M
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
1CUP
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BU of 1cup by Molmil
METHIONINE CORE MUTANT OF T4 LYSOZYME
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 (1.89 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
200L
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BU of 200l by Molmil
THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, LYSOZYME
Authors:Baldwin, E, Xu, J, Hajiseyedjavadi, O, Matthews, B.W.
Deposit date:1995-11-06
Release date:1996-03-08
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.95 Å)
Cite:Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme.
J.Mol.Biol., 259, 1996
221L
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BU of 221l by Molmil
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Blaber, M, Matthews, B.W.
Deposit date:1993-05-28
Release date:1994-01-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Biochemistry, 32, 1993
1HN1
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BU of 1hn1 by Molmil
E. COLI (LAC Z) BETA-GALACTOSIDASE (ORTHORHOMBIC)
Descriptor: BETA-GALACTOSIDASE, MAGNESIUM ION, SODIUM ION
Authors:Juers, D.H, Matthews, B.W.
Deposit date:2000-12-05
Release date:2001-12-12
Last modified:2023-08-09
Method:X-RAY DIFFRACTION (3 Å)
Cite:Reversible lattice repacking illustrates the temperature dependence of macromolecular interactions.
J.Mol.Biol., 311, 2001
2OE9
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BU of 2oe9 by Molmil
High-pressure structure of pseudo-WT T4 Lysozyme
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, Lysozyme
Authors:Collins, M.D, Quillin, M.L, Matthews, B.W, Gruner, S.M.
Deposit date:2006-12-28
Release date:2007-01-30
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (2.01 Å)
Cite:Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography.
J.Mol.Biol., 367, 2007
2OEA
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BU of 2oea by Molmil
High-pressure structure of pseudo-WT T4 Lysozyme
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, Lysozyme
Authors:Collins, M.D, Quillin, M.L, Matthews, B.W, Gruner, S.M.
Deposit date:2006-12-28
Release date:2007-01-30
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (2.01 Å)
Cite:Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography.
J.Mol.Biol., 367, 2007
2OE7
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BU of 2oe7 by Molmil
High-Pressure T4 Lysozyme
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, Lysozyme
Authors:Collins, M.D, Quillin, M.L, Matthews, B.W, Gruner, S.M.
Deposit date:2006-12-28
Release date:2007-01-30
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography.
J.Mol.Biol., 367, 2007
1DYB
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BU of 1dyb by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.
J.Mol.Biol., 235, 1994
1DYE
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BU of 1dye by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.
J.Mol.Biol., 235, 1994
1DYA
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BU of 1dya by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.
J.Mol.Biol., 235, 1994
1DYG
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BU of 1dyg by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhou, H.-J, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.
J.Mol.Biol., 235, 1994
1DYC
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BU of 1dyc by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhang, X, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.
J.Mol.Biol., 235, 1994
1DYF
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BU of 1dyf by Molmil
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Descriptor: BETA-MERCAPTOETHANOL, CHLORIDE ION, T4 LYSOZYME
Authors:Zhou, H.-J, Matthews, B.W.
Deposit date:1993-05-13
Release date:1993-10-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.
J.Mol.Biol., 235, 1994

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