M
Michael Nilges
Researcher at Pasteur Institute
Publications - 201
Citations - 29850
Michael Nilges is an academic researcher from Pasteur Institute. The author has contributed to research in topics: Pilus & Biology. The author has an hindex of 58, co-authored 190 publications receiving 28710 citations. Previous affiliations of Michael Nilges include Max Planck Society & Centre national de la recherche scientifique.
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Journal ArticleDOI
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Axel T. Brunger,Axel T. Brunger,Paul D. Adams,G M Clore,W. L. DeLano,Piet Gros,R.W. Grosse-Kunstleve,R.W. Grosse-Kunstleve,Jiansheng Jiang,J. Kuszewski,Michael Nilges,Navraj S. Pannu,Randy J. Read,Luke M. Rice,Thomas Simonson,Gregory L. Warren +15 more
TL;DR: The Crystallography & NMR System (CNS) as mentioned in this paper is a software suite for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy.
Journal ArticleDOI
Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations.
TL;DR: It is shown that the hybrid method is more efficient computationally and samples a larger region of conformational space consistent with the experimental data than full metric matrix distance geometry calculations alone, particularly for large systems.
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Refinement of protein structures in explicit solvent.
Jens P. Linge,Mark A. Williams,Christian A.E.M. Spronk,Alexandre M. J. J. Bonvin,Michael Nilges +4 more
TL;DR: The results demonstrate the significant improvement of structure quality by a short refinement in a thin layer of solvent and show that a dihedral angle energy term in the force field is beneficial for structure calculation and refinement.
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Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2.
TL;DR: An automated method, based on the principle of simulated annealing, is presented for determining the three-dimensional structures of proteins on the basis of short (less than 5 A) interproton distance data derived from nuclear Overhauser enhancement (NOE) measurements.
Journal ArticleDOI
ARIA2: Automated NOE assignment and data integration in NMR structure calculation
Wolfgang Rieping,Michael Habeck,Benjamin Bardiaux,Aymeric Bernard,Thérèse E. Malliavin,Michael Nilges +5 more
TL;DR: This work presents version 2.1 of ARIA (Ambiguous Restraints for Iterative Assignment) for automated assignment of nuclear Overhauser enhancement (NOE) data and NMR structure calculation and reports on recent developments, most notably a graphical user interface.