Sheldrick, George M.

[["dc.bibliographiccitation.firstpage","393"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","395"],["dc.bibliographiccitation.volume","59"],["dc.contributor.author","Debreczeni, J. E."],["dc.contributor.author","Bunkoczi, G."],["dc.contributor.author","Girmann, B."],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T10:41:00Z"],["dc.date.available","2018-11-07T10:41:00Z"],["dc.date.issued","2003"],["dc.description.abstract","SAD (single-wavelength anomalous diffraction) has enormous potential for phasing proteins using only the anomalous signal of the almost ubiquitous native sulfur, but requires extremely precise data. The previously unknown structure of the lima bean trypsin inhibitor (LBTI) was solved using highly redundant data collected to 3 Angstrom using a CCD detector with a rotating-anode generator and three-circle goniometer. The seven 'super-S' atoms (disulfide bridges) were located by dual-space recycling with SHELXD and the high solvent content enabled the density-modification program SHELXE to generate high-quality maps despite the modest resolution. Subsequently, a 2.05 Angstrom synchrotron data set was collected and used for further phase extension and structure refinement."],["dc.identifier.doi","10.1107/S0907444902020917"],["dc.identifier.isi","000180641900033"],["dc.identifier.pmid","12554963"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46440"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Munksgaard"],["dc.relation.issn","0907-4449"],["dc.title","In-house phase determination of the lima bean trypsin inhibitor: a low-resolution sulfur-SAD case"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1160"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","1164"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Bunkoczi, G."],["dc.contributor.author","Vertesy, L."],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T10:56:52Z"],["dc.date.available","2018-11-07T10:56:52Z"],["dc.date.issued","2005"],["dc.description.abstract","The amphomycin derivative tsushimycin has been crystallized and its structure determined at 1.0 angstrom resolution. The asymmetric unit contains 12 molecules and with 1300 independent atoms this structure is one of the largest solved using ab initio direct methods. The antibiotic is comprised of a cyclodecapeptide core, an exocyclic amino acid and a fatty-acid residue. Its backbone adopts a saddle-like conformation that is stabilized by a Ca2+ ion bound within the peptide ring and accounts for the Ca2+-dependence of this antibiotic class. Additional Ca2+ ions link the antibiotic molecules to dimers that enclose an empty space resembling a binding cleft. The dimers possess a large hydrophobic surface capable of interacting with the bacterial cell membrane. The antibiotic daptomycin may exhibit a similar conformation, as the amino-acid sequence is conserved at positions involved in Ca2+ binding."],["dc.identifier.doi","10.1107/S0907444905017270"],["dc.identifier.isi","000230621500018"],["dc.identifier.pmid","16041082"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50114"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","0907-4449"],["dc.title","Structure of the lipopeptide antibiotic tsushimycin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","688"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","696"],["dc.bibliographiccitation.volume","59"],["dc.contributor.author","Debreczeni, J. E."],["dc.contributor.author","Bunkoczi, G."],["dc.contributor.author","Ma, Q. J."],["dc.contributor.author","Blaser, H."],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T10:39:34Z"],["dc.date.available","2018-11-07T10:39:34Z"],["dc.date.issued","2003"],["dc.description.abstract","Five test structures (orthorhombic and trigonal trypsin, cubic and rhombohedral insulin and thaumatin) have been solved by the SAD (single-wavelength anomalous diffraction) method using highly redundant data collected at 100 K with a CCD detector, rotating-anode generator and three-circle goniometer. The very weak anomalous scattering (primarily from sulfur) was sufficient to locate all the anomalous scatterers using the integrated direct and Patterson methods in SHELXD. These positions and occupancies were used without further refinement to estimate phases that were extended to native (in-house) resolution by the sphere of influence algorithm in SHELXE. The final map correlation coefficients relative to the anisotropically refined structures were in the range 0.81-0.97. The use of highly redundant medium-resolution laboratory data for sulfur-SAD phasing combined with high-resolution synchrotron native data for phase expansion and structure refinement clearly has considerable potential."],["dc.identifier.doi","10.1107/S0907444903002646"],["dc.identifier.isi","000181815600010"],["dc.identifier.pmid","12657788"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46083"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0907-4449"],["dc.title","In-house measurement of the sulfur anomalous signal and its use for phasing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","723"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","732"],["dc.bibliographiccitation.volume","318"],["dc.contributor.author","Lehmann, C."],["dc.contributor.author","Bunkoczi, G."],["dc.contributor.author","Vertesy, L."],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T10:29:55Z"],["dc.date.available","2018-11-07T10:29:55Z"],["dc.date.issued","2002"],["dc.description.abstract","The vancomycin-related antibiotics balhimycin and degluco-balhimycin have been crystallized in complexes with di-, tri- and pentapeptides that emulate bacterial cell-wall precursors, and four structures determined at atomic resolution (< 1 Angstrom). In addition to the features expected from previous structural and spectroscopic studies, two new motifs were observed that may prove important in the design of antibiotics modified to overcome bacterial resistance. A changed binding mode was found in two dipeptide complexes, and a new type of face-to-face oligomerization (in addition to the well-established back-to-back dimerization) was seen when the model peptide reaches a critical fraction of the size of the cell-wall precursor pentapeptide. The extensive interactions involving both antibiotic and peptide molecules in this interface should appreciably enhance the kinetic and thermodynamic stability of the complexes. In the pentapeptide complex, the relative positions of the peptides are close to those required for D-Ala elimination, so this structure may provide a realistic model for the prevention of the enzyme-catalyzed cell-wall crosslinking by antibiotic binding. (C) 2002 Elsevier Science Ltd. All rights reserved."],["dc.identifier.doi","10.1016/S0022-2836(02)00146-8"],["dc.identifier.isi","000175767700010"],["dc.identifier.pmid","12054818"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43747"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Ltd Elsevier Science Ltd"],["dc.relation.issn","0022-2836"],["dc.title","Structures of glycopeptide antibiotics with peptides that model bacterial cell-wall precursors"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","745"],["dc.bibliographiccitation.issue","11-12"],["dc.bibliographiccitation.journal","Journal of Peptide Science"],["dc.bibliographiccitation.lastpage","752"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Bunkoczi, G."],["dc.contributor.author","Schiell, M."],["dc.contributor.author","Vertesy, L."],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T10:35:05Z"],["dc.date.available","2018-11-07T10:35:05Z"],["dc.date.issued","2003"],["dc.description.abstract","The crystal structures of the peptaibol antibiotics cephaibol A, cephaibol B and cephaibol C have been determined at ca. 0.9 Angstrom resolution. All three adopt a helical conformation With a sharp bend (of about 55degrees) at the central hydroxyproline. All isovalines were found to possess the D configuration, superposition of all four models (there are two independent molecules in the cephaibol B structure) shows that the N-terminal helix is rigid and the C-terminus is flexible. There are differences in the hydrogen bonding patterns for the three structures that crystallize in different space groups despite relatively similar unit cell dimensions, but only in the case of cephaibol C does the packing emulate the formation of a membrane channel believed to be important for their biological function. Copyright (C) 2003 European Peptide Society and John Wiley Sons. Ltd."],["dc.identifier.doi","10.1002/psc.496"],["dc.identifier.isi","000186842400010"],["dc.identifier.pmid","14658793"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45014"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","John Wiley & Sons Ltd"],["dc.publisher.place","Chichester"],["dc.relation.conference","Peptaibols Workshop"],["dc.relation.eventlocation","JENA, GERMANY"],["dc.relation.issn","1075-2617"],["dc.title","Crystal structures of cephaibols"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1340"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","1342"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Bunkoczi, G."],["dc.contributor.author","Vertesy, L."],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T08:33:36Z"],["dc.date.available","2018-11-07T08:33:36Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1002/anie.200461933"],["dc.identifier.isi","000227266500006"],["dc.identifier.pmid","15674989"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17614"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1433-7851"],["dc.title","The antiviral antibiotic feglymycin: First direct-methods solution of a 1000+equal-atom structure"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]