K
Kim Henrick
Researcher at European Bioinformatics Institute
Publications - 173
Citations - 21371
Kim Henrick is an academic researcher from European Bioinformatics Institute. The author has contributed to research in topics: Crystal structure & Protein Data Bank. The author has an hindex of 35, co-authored 173 publications receiving 19158 citations. Previous affiliations of Kim Henrick include Imperial College London & Rutgers University.
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Journal ArticleDOI
Inference of macromolecular assemblies from crystalline state.
E. Krissinel,Kim Henrick +1 more
TL;DR: A new method, based on chemical thermodynamics, is developed for automatic detection of macromolecular assemblies in the Protein Data Bank (PDB) entries that are the results of X-ray diffraction experiments, as found, biological units may be recovered at 80-90% success rate, which makesX-ray crystallography an important source of experimental data on macromolescular complexes and protein-protein interactions.
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Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
E. Krissinel,Kim Henrick +1 more
TL;DR: The present paper describes the SSM algorithm of protein structure comparison in three dimensions, which includes an original procedure of matching graphs built on the protein's secondary-structure elements, followed by an iterative three-dimensional alignment of protein backbone Calpha atoms.
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Announcing the worldwide Protein Data Bank.
TL;DR: The creation of the wwPDB formalizes the international character of the PDB and ensures that the archive remains single and uniform, and provides a mechanism to ensure consistent data for software developers and users worldwide.
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The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data
TL;DR: The worldwide Protein Data Bank (wwPDB) is the international collaboration that manages the deposition, processing and distribution of the PDB archive, a repository for the coordinates and related information for more than 38 000 structures, including proteins, nucleic acids and large macromolecular complexes that have been determined using X-ray crystallography, NMR and electron microscopy techniques.
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CAPRI: A Critical Assessment of PRedicted Interactions
Joël Janin,Kim Henrick,John Moult,Lynn F. Ten Eyck,Michael J.E. Sternberg,Sandor Vajda,Ilya A. Vakser,Shoshana J. Wodak +7 more
TL;DR: The motivations for launching CAPRI, the rules that were applied to select targets and run the experiment, the results stress the need for new scoring functions and for methods handling the conformation changes that were observed in some of the target systems, and some conclusions can already be drawn.