Author results

1L23
  • Download 1l23
  • View 1l23
Molmil generated image of 1l23
ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
Descriptor:T4 LYSOZYME
Authors:Nicholson, H., Matthews, B.W.
Deposit date:1989-05-01
Release date:1990-01-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
Proc.Natl.Acad.Sci.USA, 84, 1987
1L24
  • Download 1l24
  • View 1l24
Molmil generated image of 1l24
ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
Descriptor:T4 LYSOZYME
Authors:Nicholson, H., Matthews, B.W.
Deposit date:1989-05-01
Release date:1990-01-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
Proc.Natl.Acad.Sci.USA, 84, 1987
7TLN
  • Download 7tln
  • View 7tln
Molmil generated image of 7tln
STRUCTURAL ANALYSIS OF THE INHIBITION OF THERMOLYSIN BY AN ACTIVE-SITE-DIRECTED IRREVERSIBLE INHIBITOR
Descriptor:THERMOLYSIN, CALCIUM ION, ZINC ION, ...
Authors:Matthews, B.W., Holmes, M.A., Tronrud, D.E.
Deposit date:1983-01-27
Release date:1983-03-09
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor.
Biochemistry, 22, 1983
4TLN
  • Download 4tln
  • View 4tln
Molmil generated image of 4tln
BINDING OF HYDROXAMIC ACID INHIBITORS TO CRYSTALLINE THERMOLYSIN SUGGESTS A PENTACOORDINATE ZINC INTERMEDIATE IN CATALYSIS
Descriptor:THERMOLYSIN, CALCIUM ION, ZINC ION, ...
Authors:Matthews, B.W., Holmes, M.A.
Deposit date:1982-02-08
Release date:1982-05-26
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis.
Biochemistry, 20, 1981
5TLN
  • Download 5tln
  • View 5tln
Molmil generated image of 5tln
BINDING OF HYDROXAMIC ACID INHIBITORS TO CRYSTALLINE THERMOLYSIN SUGGESTS A PENTACOORDINATE ZINC INTERMEDIATE IN CATALYSIS
Descriptor:THERMOLYSIN, CALCIUM ION, ZINC ION, ...
Authors:Matthews, B.W., Holmes, M.A.
Deposit date:1982-02-08
Release date:1982-05-26
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis.
Biochemistry, 20, 1981
4LZM
  • Download 4lzm
  • View 4lzm
Molmil generated image of 4lzm
COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS
Descriptor:T4 LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL
Authors:Bell, J.A., Wilson, K., Zhang, X.-J., Faber, H.R., Nicholson, H., Matthews, B.W.
Deposit date:1991-01-25
Release date:1992-07-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths.
Proteins, 10, 1991
5LZM
  • Download 5lzm
  • View 5lzm
Molmil generated image of 5lzm
COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS
Descriptor:T4 LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL
Authors:Bell, J.A., Wilson, K., Zhang, X.-J., Faber, H.R., Nicholson, H., Matthews, B.W.
Deposit date:1991-01-25
Release date:1992-07-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths.
Proteins, 10, 1991
6LZM
  • Download 6lzm
  • View 6lzm
Molmil generated image of 6lzm
COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS
Descriptor:T4 LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL
Authors:Bell, J.A., Wilson, K., Zhang, X.-J., Faber, H.R., Nicholson, H., Matthews, B.W.
Deposit date:1991-01-25
Release date:1992-07-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths.
Proteins, 10, 1991
7LZM
  • Download 7lzm
  • View 7lzm
Molmil generated image of 7lzm
COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS
Descriptor:T4 LYSOZYME, CHLORIDE ION
Authors:Bell, J.A., Wilson, K., Zhang, X.-J., Faber, H.R., Nicholson, H., Matthews, B.W.
Deposit date:1991-01-25
Release date:1992-07-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths.
Proteins, 10, 1991
1L36
  • Download 1l36
  • View 1l36
Molmil generated image of 1l36
TOWARD A SIMPLIFICATION OF THE PROTEIN FOLDING PROBLEM: A STABILIZING POLYALANINE ALPHA-HELIX ENGINEERED IN T4 LYSOZYME
Descriptor:LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL
Authors:Zhang, X.-J., Baase, W.A., Matthews, B.W.
Deposit date:1990-12-26
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme.
Biochemistry, 30, 1991
1L37
  • Download 1l37
  • View 1l37
Molmil generated image of 1l37
CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Biochemistry, 30, 1991
1L38
  • Download 1l38
  • View 1l38
Molmil generated image of 1l38
CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Biochemistry, 30, 1991
1L39
  • Download 1l39
  • View 1l39
Molmil generated image of 1l39
CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Biochemistry, 30, 1991
1L40
  • Download 1l40
  • View 1l40
Molmil generated image of 1l40
CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Biochemistry, 30, 1991
1L41
  • Download 1l41
  • View 1l41
Molmil generated image of 1l41
CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.75 Å)
Cite:Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Biochemistry, 30, 1991
1L42
  • Download 1l42
  • View 1l42
Molmil generated image of 1l42
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L43
  • Download 1l43
  • View 1l43
Molmil generated image of 1l43
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L44
  • Download 1l44
  • View 1l44
Molmil generated image of 1l44
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L45
  • Download 1l45
  • View 1l45
Molmil generated image of 1l45
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L46
  • Download 1l46
  • View 1l46
Molmil generated image of 1l46
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L47
  • Download 1l47
  • View 1l47
Molmil generated image of 1l47
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221, 1991
1L48
  • Download 1l48
  • View 1l48
Molmil generated image of 1l48
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor:T4 LYSOZYME, BETA-MERCAPTOETHANOL
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
J.Mol.Biol., 221, 1991
1L49
  • Download 1l49
  • View 1l49
Molmil generated image of 1l49
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
J.Mol.Biol., 221, 1991
1L50
  • Download 1l50
  • View 1l50
Molmil generated image of 1l50
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
J.Mol.Biol., 221, 1991
1L51
  • Download 1l51
  • View 1l51
Molmil generated image of 1l51
STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA-HELICES IN BACTERIOPHAGE T4 LYSOZYME
Descriptor:T4 LYSOZYME
Authors:Daopin, S., Matthews, B.W.
Deposit date:1991-01-28
Release date:1991-10-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
J.Mol.Biol., 221, 1991