Sheldrick, George M.

[["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","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","s44"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica. Section A, Foundations and Advances"],["dc.bibliographiccitation.lastpage","s44"],["dc.bibliographiccitation.volume","71"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Hahn, Hinrich W."],["dc.contributor.author","Luebben, Anna V."],["dc.contributor.author","Meilleur, Flora"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Köpfer, David A."],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Luebben, Jens"],["dc.date.accessioned","2021-03-05T08:58:58Z"],["dc.date.available","2021-03-05T08:58:58Z"],["dc.date.issued","2015"],["dc.identifier.doi","10.1107/S2053273315099301"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80318"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","2053-2733"],["dc.title","Xen crystallography - choose your radiation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3976"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","3984"],["dc.bibliographiccitation.volume","284"],["dc.contributor.author","Pal, Aritra"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Grapp, Marcel"],["dc.contributor.author","Schreiber, Kathrin"],["dc.contributor.author","Gronborg, Mads"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Steinfeld, Robert"],["dc.date.accessioned","2017-09-07T11:47:33Z"],["dc.date.available","2017-09-07T11:47:33Z"],["dc.date.issued","2009"],["dc.description.abstract","Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I. We show that purified TPP1 requires at least partial glycosylation for in vitro autoprocessing and proteolytic activity. We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain. X-ray crystallographic analysis at 2.35 angstrom resolution reveals a globular structure with a subtilisin-like fold, a Ser(475) -Glu(272) -Asp(360) catalytic triad, and an octahedrally coordinated Ca(2+) -binding site that are characteristic features of the S53 sedolisin family of peptidases. In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins. Two alternative conformations of the catalytic Asp(276) are associated with the activation status of TPP1. 28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis."],["dc.identifier.doi","10.1074/jbc.M806947200"],["dc.identifier.gro","3143151"],["dc.identifier.isi","000262872500066"],["dc.identifier.pmid","19038966"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/633"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Fonds der Chemischen Industrie"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Structure of Tripeptidyl-peptidase I Provides Insight into the Molecular Basis of Late Infantile Neuronal Ceroid Lipofuscinosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","945"],["dc.bibliographiccitation.issue","9-10"],["dc.bibliographiccitation.journal","Zeitschrift für Naturforschung B"],["dc.bibliographiccitation.lastpage","949"],["dc.bibliographiccitation.volume","69"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","ZlatopolsIdybe, Boris D."],["dc.contributor.author","Kozhushkov, Sergei I."],["dc.contributor.author","Meijere, Armin de"],["dc.date.accessioned","2018-11-07T09:33:55Z"],["dc.date.available","2018-11-07T09:33:55Z"],["dc.date.issued","2014"],["dc.description.abstract","The structure of hormaomycin has been determined in two crystals grown under different conditions, i. e. in the absence and in the presence of magnesium chloride. In both crystals, the macrocyclic hexadepsipeptide assumes a rather flat conformation, and the dipeptide side chain resides in the same equatorial plane. This is a significant difference in comparison with the compact bent conformation of hormaomycin in solution, as previously determined by an extensive NMR study."],["dc.identifier.doi","10.5560/ZNB.2014-4116"],["dc.identifier.isi","000347145200001"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32066"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.issn","1865-7117"],["dc.relation.issn","0932-0776"],["dc.title","Structure of Hormaomycin, a Naturally Occurring Cyclic Octadepsipeptide, in the Crystal"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION A"],["dc.bibliographiccitation.lastpage","8"],["dc.bibliographiccitation.volume","67"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T09:00:34Z"],["dc.date.available","2018-11-07T09:00:34Z"],["dc.date.issued","2011"],["dc.description.abstract","Medium- to high-resolution X-ray structures of DNA and RNA molecules were investigated to find geometric properties useful for automated model building in crystallographic electron-density maps. We describe a simple method, starting from a list of electron-density 'blobs', for identifying backbone phosphates and nucleic acid bases based on properties of the local electron-density distribution. This knowledge should be useful for the automated building of nucleic acid models into electron-density maps. We show that the distances and angles involving C1' and the P atoms, using the pseudo-torsion angles eta' and theta' that describe the ... P-C1'-P-C1' ... chain, provide a promising basis for building the nucleic acid polymer. These quantities show reasonably narrow distributions with asymmetry that should allow the direction of the phosphate backbone to be established."],["dc.identifier.doi","10.1107/S0108767310039140"],["dc.identifier.isi","000285520100001"],["dc.identifier.pmid","21173468"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24196"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0108-7673"],["dc.title","Geometric properties of nucleic acids with potential for autobuilding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","118a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Kopfer, David A."],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","de Groot, Bert L."],["dc.date.accessioned","2018-11-07T10:01:55Z"],["dc.date.available","2018-11-07T10:01:55Z"],["dc.date.issued","2015"],["dc.format.extent","118A"],["dc.identifier.doi","10.1016/j.bpj.2014.11.663"],["dc.identifier.isi","000359471700591"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38130"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Ion Permeation in Potassium Channels Involves Direct Coulomb Knock-On between Ions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","129a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Sansom, Mark S. P."],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Köpfer, David A."],["dc.date.accessioned","2018-11-07T10:01:56Z"],["dc.date.available","2018-11-07T10:01:56Z"],["dc.date.issued","2015"],["dc.format.extent","129A"],["dc.identifier.doi","10.1016/j.bpj.2014.11.721"],["dc.identifier.isi","000359471700647"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38131"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Direct Contacts of K+ Ions in the Selectivity Filter Enable the High Conductance of K+ Channels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","352"],["dc.bibliographiccitation.issue","6207"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","355"],["dc.bibliographiccitation.volume","346"],["dc.contributor.author","Koepfer, David A."],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","de Groot, Bert L."],["dc.date.accessioned","2018-11-07T09:33:31Z"],["dc.date.available","2018-11-07T09:33:31Z"],["dc.date.issued","2014"],["dc.description.abstract","Potassium channels selectively conduct K+ ions across cellular membranes with extraordinary efficiency. Their selectivity filter exhibits four binding sites with approximately equal electron density in crystal structures with high K+ concentrations, previously thought to reflect a superposition of alternating ion-and water-occupied states. Consequently, cotranslocation of ions with water has become a widely accepted ion conduction mechanism for potassium channels. By analyzing more than 1300 permeation events from molecular dynamics simulations at physiological voltages, we observed instead that permeation occurs via ion-ion contacts between neighboring K+ ions. Coulomb repulsion between adjacent ions is found to be the key to high-efficiency K+ conduction. Crystallographic data are consistent with directly neighboring K+ ions in the selectivity filter, and our model offers an intuitive explanation for the high throughput rates of K+ channels."],["dc.identifier.doi","10.1126/science.1254840"],["dc.identifier.isi","000343041100045"],["dc.identifier.pmid","25324389"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31983"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.issn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.title","Ion permeation in K+ channels occurs by direct Coulomb knock-on"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","570"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","581"],["dc.bibliographiccitation.volume","376"],["dc.contributor.author","Schlicker, Christine"],["dc.contributor.author","Fokina, Oleksandra"],["dc.contributor.author","Kioft, Nicole"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Forchhammer, Karl"],["dc.date.accessioned","2018-11-07T11:18:18Z"],["dc.date.available","2018-11-07T11:18:18Z"],["dc.date.issued","2008"],["dc.description.abstract","The homologue of the phosphoprotein I'll phosphatase PphA from Thermosynechococcus elongatus, termed tPphA, was identified and its structure was resolved in two different space groups, C222(1) and P4(1)2(1)2, at a resolution of 1.28 and 3.05 angstrom, respectively. tPphA belongs to a large and widely distributed subfamily of Mg2+/Mn2+-dependent phosphatases of the PPM superfamily characterized by the lack of catalytic and regulatory domains. The core structure of tPphA shows a high degree of similarity to the two PPM structures identified so far. In contrast to human PP2C, but similar to Mycobacterium tuberculosis phosphatase PstP, the catalytic centre exhibits a third metal ion in addition to the dinuclear metal centre universally conserved in all PPM members. The fact that the third metal is only liganded by amino acids, which are universally conserved in all PPM members, implies that the third metal could be general for all members of this family. As a specific feature of tPphA, a flexible subdomain, previously recognized as a flap domain, could be revealed. Comparison of different structural isomers of tPphA as well as site-specific mutagenesis implied that the flap domain is involved in substrate binding and catalytic activity. The structural arrangement of the flap domain was accompanied by a large side-chain movement of an Arg residue (Arg169) at the basis of the flap. Mutation of this residue strongly impaired protein stability as well as catalytic activity, emphasizing the importance of this amino acid for the regional polysterism of the flap subdomain and confirming the assumption that flap domain flexibility is involved in catalysis. (C) 2007 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2007.11.097"],["dc.identifier.isi","000253554700023"],["dc.identifier.pmid","18164312"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55003"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Ltd Elsevier Science Ltd"],["dc.relation.issn","0022-2836"],["dc.title","Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: A flexible flap subdomain controls access to the catalytic site"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]