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George M. Sheldrick

Researcher at University of Göttingen

Publications -  794
Citations -  170469

George M. Sheldrick is an academic researcher from University of Göttingen. The author has contributed to research in topics: Crystal structure & Molecule. The author has an hindex of 58, co-authored 791 publications receiving 151229 citations. Previous affiliations of George M. Sheldrick include University of Regensburg.

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Nitrosyl coupling in transition metal complexes: the molecular structure of [(Ph3P)2Pt(N2O2)]

TL;DR: A crystallographic study of [(Ph3P)2Pt(N2O2)] showed that the two NO groups are coupled via the nitrogen atoms, forming a cis-hyponitrite ligand, which bonds to platinum through the oxygen atoms to give a [graphic omitted] ring.
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The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin : A tale with a twist

TL;DR: This work presents the first structures (two X-ray models and an NMR-derived model) of the (2)F 1(3)F1 module pair, which forms part of the binding site for Fn-binding proteins from pathogenic bacteria, and underlines the benefits of combiningX-ray and NMR data in the studies of multi-domain proteins.
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Di- and tetra-nuclear complexes with bis(diphenylphosphino)amide and bis(diphenylphosphino)methanide as bi- and tri-dentate ligands. X-Ray structures of [(Ph3P)(O3ClO)AgN(Ph2PAuPPh2)2NAg(OClO3)(PPh3)] and [(C6F5)AuCH(Ph2PAuPPh2)2ChAu(C6F5)]

TL;DR: AuCl(CH2PR3) as discussed by the authors gives neutral tetranuclear derivatives, ring systems in which the amido or methanido ligands are tridentate (confirmed by X-ray structures of two products).
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Structures of Complexes between Echinomycin and Duplex DNA.

TL;DR: The structure of the bis-intercalation complex of the depsipeptide antibiotic echinomycin with (CGTACG)2 has been redetermined at a higher resolution and new high-resolution structures are reported, providing more precise details of the hydrogen bonding and other interactions between the bis -intercalating antibiotics and the duplex DNA than were previously available.
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Crystal structure and functional analysis of drosophila wind - a protein-disulfide isomerase-related protein

TL;DR: The three-dimensional structure of Wind is described at 1.9-Å resolution and a candidate surface for interaction with Pipe is identified and represents the first crystal structure of a eukaryotic protein-disulfide isomerase-related protein of the endoplasmic reticulum to be described.