The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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In: Journal of Molecular Biology ; 217 (1991), 3. - S. 541-549. - ISSN 0022-2836. - eISSN 1089-8638
- Classification
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Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
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Bibliothek der Universität Konstanz
- (when)
-
2012
- Creator
- URN
-
urn:nbn:de:bsz:352-208677
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:51 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Diederichs, Kay
- Schulz, Georg E.
- Bibliothek der Universität Konstanz
Time of origin
- 2012
Other Objects (12)
Three-Dimensional Structure of the Complex between the Mitochondrial Matrix Adenylate Kinase and Its Substrate AMP
Induced-fit movements in adenylate kinases
A comparison of some heavy-atom refinement and phasing programs in a test case
Structural superposition of proteins with unknown alignment and detection of topological similarity using a six-dimensional search algorithm
SUPERIMPOSE - a program for the unambiguous structural superposition of spatially related molecules, including macromolecules
Computing in macromolecular crystallography using a parallel architecture
Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach
Quantifying instrument errors in macromolecular X-ray data sets
Structure of the outer membrane protein FhuA presents a binding mode for Lipopolysaccharide
Dissecting random and systematic differences between noisy composite data sets
Some aspects of quantitative analysis and correction of radiation damage
Refined Crystal Structure and Mutagenesis of Human Granulocyte-Macrophage Colony-Stimulating Factor
Three-Dimensional Structure of the Complex between the Mitochondrial Matrix Adenylate Kinase and Its Substrate AMP
Induced-fit movements in adenylate kinases
A comparison of some heavy-atom refinement and phasing programs in a test case
Structural superposition of proteins with unknown alignment and detection of topological similarity using a six-dimensional search algorithm
SUPERIMPOSE - a program for the unambiguous structural superposition of spatially related molecules, including macromolecules
Computing in macromolecular crystallography using a parallel architecture
Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach
Quantifying instrument errors in macromolecular X-ray data sets
Structure of the outer membrane protein FhuA presents a binding mode for Lipopolysaccharide
Dissecting random and systematic differences between noisy composite data sets
Some aspects of quantitative analysis and correction of radiation damage
Refined Crystal Structure and Mutagenesis of Human Granulocyte-Macrophage Colony-Stimulating Factor
Three-Dimensional Structure of the Complex between the Mitochondrial Matrix Adenylate Kinase and Its Substrate AMP
Induced-fit movements in adenylate kinases
A comparison of some heavy-atom refinement and phasing programs in a test case
Structural superposition of proteins with unknown alignment and detection of topological similarity using a six-dimensional search algorithm
SUPERIMPOSE - a program for the unambiguous structural superposition of spatially related molecules, including macromolecules
Computing in macromolecular crystallography using a parallel architecture
Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach
Quantifying instrument errors in macromolecular X-ray data sets
Structure of the outer membrane protein FhuA presents a binding mode for Lipopolysaccharide
Dissecting random and systematic differences between noisy composite data sets
Some aspects of quantitative analysis and correction of radiation damage