Sheldrick, George M.

[["dc.bibliographiccitation.firstpage","3"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations and Advances"],["dc.bibliographiccitation.lastpage","8"],["dc.bibliographiccitation.volume","71"],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T10:02:25Z"],["dc.date.available","2018-11-07T10:02:25Z"],["dc.date.issued","2015"],["dc.description.abstract","The new computer program SHELXT employs a novel dual-space algorithm to solve the phase problem for single-crystal reflection data expanded to the space group P1. Missing data are taken into account and the resolution extended if necessary. All space groups in the specified Laue group are tested to find which are consistent with the P1 phases. After applying the resulting origin shifts and space-group symmetry, the solutions are subject to further dual-space recycling followed by a peak search and summation of the electron density around each peak. Elements are assigned to give the best fit to the integrated peak densities and if necessary additional elements are considered. An isotropic refinement is followed for non-centrosymmetric space groups by the calculation of a Flack parameter and, if appropriate, inversion of the structure. The structure is assembled to maximize its connectivity and centred optimally in the unit cell. SHELXT has already solved many thousand structures with a high success rate, and is optimized for multiprocessor computers. It is, however, unsuitable for severely disordered and twinned structures because it is based on the assumption that the structure consists of atoms."],["dc.description.sponsorship","Volkswagen-Stiftung; state of Niedersachsen"],["dc.identifier.doi","10.1107/S2053273314026370"],["dc.identifier.isi","000350545100002"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38219"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Int Union Crystallography"],["dc.relation.issn","2053-2733"],["dc.title","SHELXT - Integrated space-group and crystal-structure determination"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11854"],["dc.bibliographiccitation.issue","48"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","11862"],["dc.bibliographiccitation.volume","123"],["dc.contributor.author","Anibarro, M."],["dc.contributor.author","Gessler, K."],["dc.contributor.author","Uson, I."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Harata, K."],["dc.contributor.author","Uekama, K."],["dc.contributor.author","Hirayama, F."],["dc.contributor.author","Abe, Y."],["dc.contributor.author","Saenger, W."],["dc.date.accessioned","2018-11-07T11:19:49Z"],["dc.date.available","2018-11-07T11:19:49Z"],["dc.date.issued","2001"],["dc.description.abstract","The molecular structures of peracylated beta -cyclodextrins (CDs)-heptakis(2,3,6-tri-O-acetyl)-beta -CD (TA), heptakis(2,3,6-tri-O-propanoyl)-beta -CD (TP), and heptakis(2,3,6-tri-O-butanoyl)-beta -CD (TB)-have been determined by single crystal X-ray structure analysis. Due to the lack of O2(...)O3 ' hydrogen bonds between adjacent glucose units of the peracylated CDs, the macrocycles are elliptically distorted into nonplanar boat-shaped structures. The glucose units are tilted with respect to the O4 plane to relieve steric hindrance between adjacent acyl chains. In TB, all glucose units adopt the common C-4(1)-chair conformation and one butanoyl chain intramolecularly penetrates the cavity, whereas, in TA and TP, one glucose unit each occurs in S-O(2)-skew-boat conformation and one acyl chain closes the O6 side like a lid. In each of the three homologous molecules the intramolecular self-inclusion and lidlike orientation of acyl chains forces the associated O5-C5-C6-O6 torsion angle into a trans-conformation never observed before for unsubstituted CD; the inclusion behavior of TA, TP, and TB in solution has been studied by circular dichroism spectroscopy with the drug molsidomine and several organic compounds. No inclusion complexes are formed, which is attributed to the intramolecular closure of the molecular cavity by one of the acyl chains."],["dc.identifier.doi","10.1021/ja010696b"],["dc.identifier.isi","000172591000004"],["dc.identifier.pmid","11724591"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55377"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0002-7863"],["dc.title","Effect of peracylation of beta-cyclodextrin on the molecular structure and on the formation of inclusion complexes: An X-ray study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","no"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","ChemInform"],["dc.bibliographiccitation.lastpage","no"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","SCHAEFER, M."],["dc.contributor.author","POHL, E."],["dc.contributor.author","SCHMIDT-BAESE, K."],["dc.contributor.author","SHELDRICK, G. M."],["dc.contributor.author","HERMANN, R."],["dc.contributor.author","MALABARBA, A."],["dc.contributor.author","NEBULONI, M."],["dc.contributor.author","PELIZZI, G."],["dc.date.accessioned","2021-12-08T12:27:35Z"],["dc.date.available","2021-12-08T12:27:35Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1002/chin.199704247"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/95393"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.issn","0931-7597"],["dc.rights.uri","http://doi.wiley.com/10.1002/tdm_license_1.1"],["dc.title","ChemInform Abstract: The Molecular and Crystal Structure of the Glycopeptide A-40926 Aglycone."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","387"],["dc.bibliographiccitation.journal","Journal of Applied Crystallography"],["dc.bibliographiccitation.lastpage","390"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Fu, Zheng-Qing"],["dc.contributor.author","Chrzas, John"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Rose, John"],["dc.contributor.author","Wang, B."],["dc.date.accessioned","2018-11-07T11:03:34Z"],["dc.date.available","2018-11-07T11:03:34Z"],["dc.date.issued","2007"],["dc.description.abstract","A parallel algorithm has been designed for SHELXD to solve the heavy-atom partial structures of protein crystals quickly. Based on this algorithm, a program has been developed to run on high-performance multiple-CPU Linux PCs, workstations or clusters. Tests on the 32-CPU Linux cluster at SER-CAT, APS, Argonne National Laboratory, show that the parallelization dramatically speeds up the process by a factor of roughly the number of CPUs applied, leading to reliable and instant heavy-atom sites solution, which provides the practical opportunity to employ heavy-atom search as an alternative tool for anomalous scattering data quality evaluation during single/multiple-wavelength anomalous diffraction (SAD/MAD) data collection at synchrotron beamlines."],["dc.identifier.doi","10.1107/S0021889807003998"],["dc.identifier.isi","000244926900025"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51650"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","0021-8898"],["dc.title","A parallel program using SHELXD for quick heavy-atom partial structural solution on high-performance computers"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Koepfer, David"],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Zachariae, Ulrich"],["dc.date.accessioned","2020-12-10T14:22:41Z"],["dc.date.available","2020-12-10T14:22:41Z"],["dc.date.issued","2016"],["dc.format.extent","9A"],["dc.identifier.doi","10.1016/j.bpj.2015.11.101"],["dc.identifier.isi","000375093500050"],["dc.identifier.issn","0006-3495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71695"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.conference","60th Annual Meeting of the Biophysical-Society"],["dc.relation.eventlocation","Los Angeles, CA"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","The Molecular Dynamics of Ion Channel Permeation, Selectivity and Gating"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","407"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","415"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Alexopoulos, E."],["dc.contributor.author","Jares-Erijman, Elizabeth A."],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Klement, R."],["dc.contributor.author","Machinek, R."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Uson, I."],["dc.date.accessioned","2018-11-07T11:08:51Z"],["dc.date.available","2018-11-07T11:08:51Z"],["dc.date.issued","2005"],["dc.description.abstract","The formation of the complex of 7-amino-actinomycin D with potentially single-stranded DNA has been studied by X-ray crystallography in the solid state, by NMR in solution and by molecular modelling. The crystal structures of the complex with 5'-TTAG[(BrU)-U-5]T-3' provide interesting examples of MAD phasing in which the dispersive component of the MAD signal was almost certainly enhanced by radiation damage. The trigonal and orthorhombic crystal modifications both contain antibiotic molecules and DNA strands in the form of a 2:4 complex: in the orthorhombic form there is one such complex in the asymmetric unit, while in the trigonal structure there are four. In both structures the phenoxazone ring of the first drug intercalates between a BrU-G (analogous to T-G) wobble pair and a G-T pair where the T is part of a symmetry-related molecule. The chromophore of the second actinomycin intercalates between the BrU-G and G-BrU wobble pairs of the partially paired third and fourth strands. The base stacking also involves (A T) T triplets and Watson-Crick A-T pairs and leads to similar complex three-dimensional networks in both structures, with looping-out of unpaired bases. Although the available NOE constraints of a solution containing the antibiotic and d(TTTAGTTT) strands in the ratio 1:1 are insufficient to determine the structure of the complex from the NMR data alone, they are consistent with the intercalation geometry observed in the crystal structure. Molecular-dynamics (MD) trajectories starting from the 1:2 complexes observed in the crystal showed that although the thymines flanking the d(AGT) core are rather flexible and the G-T pairing is not permanently preserved, both strands remain bound to the actinomycin by strong interactions between it and the guanines between which it is sandwiched. Similar strong binding (hemi-intercalation) of the actinomycin to a single guanine was observed in the MD trajectories of a 1:1 complex. The dominant interaction is between the antibiotic and guanine, but the complexes are stabilized further by promiscuous base-pairing."],["dc.description.sponsorship","ICREA"],["dc.identifier.doi","10.1107/S090744490500082X"],["dc.identifier.isi","000227867600007"],["dc.identifier.pmid","15805595"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52882"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Munksgaard"],["dc.relation.issn","0907-4449"],["dc.title","Crystal and solution structures of 7-amino-actinomycin D complexes with d(TTAGBrUT), d(TTAGTT) and d(TTTAGTTT)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1448"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","1461"],["dc.bibliographiccitation.volume","58"],["dc.contributor.author","Thaimattam, R."],["dc.contributor.author","Tykarska, E."],["dc.contributor.author","Bierzynski, A."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Jaskolski, M."],["dc.date.accessioned","2018-11-07T10:03:20Z"],["dc.date.available","2018-11-07T10:03:20Z"],["dc.date.issued","2002"],["dc.description.abstract","CMTI-I, a small-protein trypsin inhibitor, has been crystallized as a 4:1 protein-zinc complex. The metal is coordinated in a symmetric tetrahedral fashion by glutamate/glutamic acid side chains. The structure was solved by direct methods in the absence of prior knowledge of the special position metal centre and refined with anisotropic displacement parameters using diffraction data extending to 1.03 Angstrom. In the final calculations, the main-chain atoms of low B-eq values were refined without restraint control. The two molecules in the asymmetric unit have a conformation that is very similar to that reported earlier for CMTI-I in complex with trypsin, despite the Met8Leu mutation of the present variant. The only significant differences are in the enzyme-binding epitope (including the Arg5 residue) and in a higher mobility loop around Glu24. The present crystal structure contains organic solvent molecules (glycerol, MPD) that interact with the inhibitor molecules in an area that is at the enzyme-inhibitor interface in the CMTI-I-trypsin complex. A perfectly ordered residue (Ala18) has an unusual Ramachandran conformation as a result of geometrical strain introduced by the three disulfide bridges that clamp the protein fold. The results confirm deficiencies of some stereochemical restraints, such as peptide planarity or the N-C-alpha-C angle, and suggest a link between their violations and hydrogen bonding."],["dc.identifier.doi","10.1107/S0907444902011769"],["dc.identifier.isi","000177624600009"],["dc.identifier.pmid","12198301"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38439"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Munksgaard"],["dc.relation.issn","0907-4449"],["dc.title","Atomic resolution structure of squash trypsin inhibitor: unexpected metal coordination"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","985"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","992"],["dc.bibliographiccitation.volume","64"],["dc.contributor.author","Pal, Aritra"],["dc.contributor.author","Debreczeni, Judit E."],["dc.contributor.author","Sevvana, Madhumati"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Kahle, Beatrix"],["dc.contributor.author","Zeeck, Axel"],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T11:11:00Z"],["dc.date.available","2018-11-07T11:11:00Z"],["dc.date.issued","2008"],["dc.description.abstract","Crystals of the cytotoxic thionin proteins viscotoxins A1 and B2 extracted from mistletoe diffracted to high resolution (1.25 and 1.05 angstrom, respectively) and are excellent candidates for testing crystallographic methods. Ab initio direct methods were only successful in solving the viscotoxin B2 structure, which with 861 unique non-H atoms is one of the largest unknown structures without an atom heavier than sulfur to be solved in this way, but sulfur-SAD phasing provided a convincing solution for viscotoxin A1. Both proteins form dimers in the crystal and viscotoxin B2 (net charge +4 per monomer), but not viscotoxin A1 (net charge +6), is coordinated by sulfate or phosphate anions. The viscotoxin A1 crystal has a higher solvent content than the viscotoxin B2 crystal (49% as opposed to 28%) with solvent channels along the crystallographic 43 axes."],["dc.identifier.doi","10.1107/S0907444908022646"],["dc.identifier.isi","000258411800011"],["dc.identifier.pmid","18703848"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53331"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0907-4449"],["dc.title","Structures of viscotoxins A1 and B2 from European mistletoe solved using native data alone"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","s219"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations and Advances"],["dc.bibliographiccitation.lastpage","s219"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Luebben, Anna V."],["dc.contributor.author","Xie, Jingwei"],["dc.contributor.author","Safaee, Nozhat"],["dc.contributor.author","Gehring, Kalle"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Dittrich, Birger"],["dc.date.accessioned","2020-12-10T18:26:02Z"],["dc.date.available","2020-12-10T18:26:02Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1107/S2053273316096686"],["dc.identifier.issn","2053-2733"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75920"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","A closer look at the parallel RNA double helix poly(rA)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","ChemInform"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Than, Ni Ni"],["dc.contributor.author","Fotso, Serge"],["dc.contributor.author","Sevvana, Madhumati"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Fiebig, Heinz H."],["dc.contributor.author","Kelter, Gerhard"],["dc.contributor.author","Laatsch, Hartmut"],["dc.date.accessioned","2021-12-08T12:29:22Z"],["dc.date.available","2021-12-08T12:29:22Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1002/chin.200527176"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/96053"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.eissn","1522-2667"],["dc.relation.issn","0931-7597"],["dc.rights.uri","http://doi.wiley.com/10.1002/tdm_license_1.1"],["dc.title","Sesquiterpene Lactones from Elephantopus scaber."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]