Sheldrick, George M.

[["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","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","1255"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","1262"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Kratzner, R."],["dc.contributor.author","Debreczeni, J. E."],["dc.contributor.author","Pape, T."],["dc.contributor.author","Schneider, Thomas R."],["dc.contributor.author","Wentzel, A."],["dc.contributor.author","Kolmar, Harald"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Uson, I."],["dc.date.accessioned","2018-11-07T10:55:49Z"],["dc.date.available","2018-11-07T10:55:49Z"],["dc.date.issued","2005"],["dc.description.abstract","The Ecballium elaterium trypsin inhibitor II (EETI-II) belongs to the family of squash inhibitors and is one of the strongest inhibitors known for trypsin. The eight independent molecules of EETI-II in the crystal structure reported here provide a good opportunity to test the hypothesis that this small cystine-knot protein (knottin) is sufficiently rigid to be used as a molecular scaffold for protein-engineering purposes. To extend this test, the structures of two complexes of EETI-II with trypsin have also been determined, one carrying a four-amino-acid mutation of EETI-II. The remarkable similarity of these structures confirms the rigidity of the molecular framework and hence its suitability as a molecular scaffold."],["dc.identifier.doi","10.1107/S0907444905021207"],["dc.identifier.isi","000231243400011"],["dc.identifier.pmid","16131759"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49872"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","0907-4449"],["dc.title","Structure of Ecballium elaterium trypsin inhibitor II (EETI-II): a rigid molecular scaffold"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3075"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Biochemistry"],["dc.bibliographiccitation.lastpage","3088"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Müller, Ilka"],["dc.contributor.author","Kahnert, A."],["dc.contributor.author","Pape, T."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Meyer-Klaucke, W."],["dc.contributor.author","Dierks, Thomas"],["dc.contributor.author","Kertesz, Michael"],["dc.contributor.author","Uson, I."],["dc.date.accessioned","2018-11-07T10:50:15Z"],["dc.date.available","2018-11-07T10:50:15Z"],["dc.date.issued","2004"],["dc.description.abstract","The alkylsulfatase AtsK from Pseudomonas putida S-313 belongs to the widespread and versatile non-heme iron(II) alpha-ketoglutarate-dependent dioxygenase superfamily and catalyzes the oxygenolytic cleavage of a variety of different alkyl sulfate esters to the corresponding aldehyde and sulfate. The enzyme is only expressed under sulfur starvation conditions, providing a selective advantage for bacterial growth in soils and rhizosphere. Here we describe the crystal structure of AtsK in the apo form and in three complexes: with the cosubstrate alpha-ketoglutarate, with alpha-ketoglutarate and iron, and finally with alpha-ketoglutarate, iron, and an alkyl sulfate ester used as substrate in catalytic studies. The overall fold of the enzyme is closely related to that of the taurine/alpha-ketoglutarate dioxygenase TauD and is similar to the fold observed for other members of the enzyme superfamily. From comparison of these structures with the crystal structure of AtsK and its complexes, we propose a general mechanism for the catalytic cycle of the alpha-ketoglutarate-dependent dioxygenase superfamily."],["dc.identifier.doi","10.1021/bi035752v"],["dc.identifier.isi","000220276700010"],["dc.identifier.pmid","15023059"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48611"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0006-2960"],["dc.title","Crystal structure of the alkylsulfatase AtsK: Insights into the catalytic mechanism of the Fe(II) alpha-ketoglutarate-dependent dioxygenase superfamily"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1427"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Carbohydrate Research"],["dc.bibliographiccitation.lastpage","1437"],["dc.bibliographiccitation.volume","339"],["dc.contributor.author","Nimz, O."],["dc.contributor.author","Gessler, K."],["dc.contributor.author","Uson, I."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Saenger, W."],["dc.date.accessioned","2018-11-07T10:48:18Z"],["dc.date.available","2018-11-07T10:48:18Z"],["dc.date.issued","2004"],["dc.description.abstract","Crystal structures are reported of cycloamylose containing 26 D-glucose residues (CA26, cyclohexaicosaose, C(156)H(260)O(130)) in complexes with undecanoic acid (CA26.2C(10)H(21)COOH.34.95H(2)O, orthorhombic P2(1)2(1)2(1), one CA26 and two bound undecanoic acids F1 and F2 in the asymmetric unit, resolution 0.95 Angstrom) and with dodecanot ((CA26)(0.5).C(12)H(25)OH.32.0H(2)O, monoclinic C2, half a CA26 binding one dodecanol, A, in the asymmetric unit, resolution 1.0 Angstrom). The macrocycle of CA26 is folded like the figure '8' into two 10 D-glucoses long left-handed V-amylose helices forming similar to5 Angstrom wide V-channels that are occupied by undecanoic acid (171, 172) or dodecanol (A) as guest molecules. The functional head groups of the guests near the 0(6) ends of the V-channels are hydrogen bonded with D-glucose O(6)(n)-H; the aliphatic termini beyond C(9) protrude from the O(2), O(3) ends. Parts of the aliphatic chains enclosed in the V-channels are all-trans except for one torsion angle each (similar to130degrees) in undecanoic acid molecules F1 and F2. There are several (guest)C-H...O hydrogen bonds to O(4) and O(6) of CA26 in both complexes, and H...H van der Waals interactions with D-glucose C(3)-H and C(5)-H dominate. C(5)-H determine the position of the aliphatic chains of undecanoic acid Fl and of dodecanol A in contrast to F2 where both C(3)-H and C(5)-H contribute equally, probably because the V-channel is narrower than in Fl and in dodecanol. Complexes of polymeric V-amylose with fatty acids and alcohols studied by X-ray fiber diffraction could not provide the here described high resolution. (C) 2004 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.carres.2004.02.030"],["dc.identifier.isi","000222077300003"],["dc.identifier.pmid","15178384"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48160"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0008-6215"],["dc.title","Inclusion complexes of V-amylose with undecanoic acid and dodecanol at atomic resolution: X-ray structures with cycloamylose containing 26 D-glucoses (cyclohexalcosaose) as host"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1971"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","1980"],["dc.bibliographiccitation.volume","60"],["dc.contributor.author","Alexopoulos, E."],["dc.contributor.author","Kusel, A."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Uson, I."],["dc.date.accessioned","2018-11-07T10:44:00Z"],["dc.date.available","2018-11-07T10:44:00Z"],["dc.date.issued","2004"],["dc.description.abstract","The crystal structure of H-(L-Tyr-d-Tyr)(4)-L-Lys-OH has been determined to 1.3 Angstrom resolution. The D, L-alternating peptide crystallizes in the tetragonal system, space group P4(3)2(1)2, with unit-cell parameters a = b = 27.99 (3), c = 78.93 (8) Angstrom. The crystals contain two molecules in the asymmetric unit that form a double-stranded right-handed antiparallel beta-helix. The structure has been solved by SIRAS using a crystal soaked in an iodide-containing solution for 1 min. The programs SHELXD and SHELXE were used to determine the iodide substructure and also the experimental electron-density map. Using the coordinates of known D,L-peptides deposited in the PDB, several attempts were made to solve the structure by molecular-replacement techniques. Although the backbone of the MR model selected shows great similarity and was used to trace the actual peptide structure in the map, it was not possible to obtain the correct solution before the experimental phases became available. The correct fragment orientations are easily determined, but the same does not apply to the translation search. Nevertheless, insights into fragment search and expansion were gained from the tests described in this paper. The correlation coefficient calculated with the resolution shell of data around 2.4 Angstrom, a distance corresponding to most 1-3 interatomic vectors, is a particularly good discriminator of correct orientations in the rotation search of small fragments."],["dc.description.sponsorship","ICREA"],["dc.identifier.doi","10.1107/S0907444904022292"],["dc.identifier.isi","000224595200007"],["dc.identifier.pmid","15502304"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/47176"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Munksgaard"],["dc.relation.issn","0907-4449"],["dc.title","Solution and structure of an alternating D,L-peptide"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","251"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Carbohydrate Research"],["dc.bibliographiccitation.lastpage","256"],["dc.bibliographiccitation.volume","333"],["dc.contributor.author","Anibarro, M."],["dc.contributor.author","Gessler, K."],["dc.contributor.author","Uson, I."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Saenger, W."],["dc.date.accessioned","2018-11-07T08:52:41Z"],["dc.date.available","2018-11-07T08:52:41Z"],["dc.date.issued","2001"],["dc.description.abstract","The inclusion complex beta -cyclodextrin 2, 7-dihydroxynaphthalene(.)4.5 H2O crystallized in the monoclinic space group P2(1), with a = 14.082(3), b = 19.079(4), c = 12.417(3) Angstrom, beta = 109.28(3)9 V = 3149.0(11) Angstrom (3), and Z = 2. An X-ray study performed at room temperature shows that the crystal packing is of the herringbone type with one 2,7-dihydroxynaphthalene included completely in the beta -CD cavity, its long axis being oriented along the B-CD molecular axis, and 4.6 water molecules are placed in the interstitial space. The beta -CD macrocycle is elliptically distorted, and the guest molecule is held in the hydrophobic beta -CD cavity by C-H . . .O and C-H . . . pi interactions. (C) 2001 Elsevier Science Ltd. All rights reserved."],["dc.identifier.doi","10.1016/S0008-6215(01)00131-8"],["dc.identifier.isi","169973600006"],["dc.identifier.pmid","11448687"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22229"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Sci Ltd"],["dc.relation.issn","0008-6215"],["dc.title","X-ray structure of beta-cyclodextrin-2,7-dihydroxy-naphthalene center dot 4.6 H2O: an unusually distorted macrocycle"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","977"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Carbohydrate Research"],["dc.bibliographiccitation.lastpage","986"],["dc.bibliographiccitation.volume","338"],["dc.contributor.author","Nimz, O."],["dc.contributor.author","Gessler, K."],["dc.contributor.author","Uson, I."],["dc.contributor.author","Laettig, S."],["dc.contributor.author","Welfle, H."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Saenger, W."],["dc.date.accessioned","2018-11-07T10:39:31Z"],["dc.date.available","2018-11-07T10:39:31Z"],["dc.date.issued","2003"],["dc.description.abstract","Cyclomaltohexaicosaose (CA26) is folded into two 1(2)/(3) turns long V-helices that are oriented antiparallel. Crystals of complexes of CA26 with NH4I3 and Ba(I-3)(2) are brown and X-ray analyses show that 13 units are located in the similar to 5 Angstrom wide central channels of the V-helices. In the complex with NH4I3, two CA26 molecules are stacked to form 2 x (1)(3) turns long channels harbouring 3 I-3(-) at 3.66-3.85 Angstrom inter I-3(-) distance (shorter than van der Waals distance, 4.3 Angstrom), whereas in the Ba(I-3)(2) complex, CA26 are not stacked and only one I-3(-) each fills the V-helices. Glucose...I contacts are formed with C5-H, C3-H, C6-H and (at the ends of the V-helices) with O6 in ( +) gauche orientation. By contrast, O2, O3, O4 and O6 in the preferred ( -) gauche orientation do not interact with I because these distances are greater than or equal to 4.01 Angstrom and exceed the van der Waals (IO)-O-... sum of radii by about 0.5 Angstrom except for one O2(...)I distance of 3.68 Angstrom near the end of one V-helix. Raman spectra indicate that the complexes share the presence of I-3(-) with blue amylose-iodine. (C) 2003 Elsevier Science Ltd. All rights reserved."],["dc.identifier.doi","10.1016/S0008-6215(03)00016-8"],["dc.identifier.isi","182442400019"],["dc.identifier.pmid","12681922"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46067"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Sci Ltd"],["dc.relation.issn","0008-6215"],["dc.title","X-ray structure of the cyclomaltohexaicosaose triiodide inclusion complex provides a model for amylose-iodine at atomic resolution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","44600"],["dc.bibliographiccitation.issue","45"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","44607"],["dc.bibliographiccitation.volume","278"],["dc.contributor.author","Ma, Q. J."],["dc.contributor.author","Guo, C. S."],["dc.contributor.author","Barnewitz, K."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Soling, H. D."],["dc.contributor.author","Uson, I."],["dc.contributor.author","Ferrari, David M."],["dc.date.accessioned","2018-11-07T10:34:47Z"],["dc.date.available","2018-11-07T10:34:47Z"],["dc.date.issued","2003"],["dc.description.abstract","In the developing Drosophila melanogaster embryo, dorsal-ventral patterning displays an absolute requirement for the product of the essential windbeutel gene, Wind. In homozygous windbeutel mutant flies, dorsal-ventral patterning fails to initiate because of the failure of the Golgi-resident proteoglycan- modifying protein, Pipe, to exit the endoplasmic reticulum, and this leads to the death of the embryo. Here, we describe the three-dimensional structure of Wind at 1.9-Angstrom resolution and identify a candidate surface for interaction with Pipe. This represents the first crystal structure of a eukaryotic protein-disulfide isomerase-related protein of the endoplasmic reticulum to be described. The dimeric protein is composed of an N-terminal thioredoxin domain and a C-terminal alpha-helical domain unique to protein-disulfide isomerase D proteins. Although Wind carries a CXXC motif that is partially surface accessible, this motif is redox inactive, and the cysteines are not required for the targeting of Pipe to the Golgi. However, both domains are required for targeting Pipe to the Golgi, and, although the mouse homologue ERp28 cannot replace the function of Wind, exchange of the Wind D-domain with that of ERp28 allows for efficient Golgi transport of Pipe."],["dc.identifier.doi","10.1074/jbc.M307966200"],["dc.identifier.isi","000186306700090"],["dc.identifier.pmid","12941941"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44950"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","37"],["dc.bibliographiccitation.lastpage","83"],["dc.bibliographiccitation.seriesnr","374"],["dc.contributor.author","Weeks, C. M."],["dc.contributor.author","Adams, P. D."],["dc.contributor.author","Berendzen, J."],["dc.contributor.author","Brunger, A. T."],["dc.contributor.author","Dodson, E. J."],["dc.contributor.author","Grosse-Kunstleve, R. W."],["dc.contributor.author","Schneider, Thomas R."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Terwilliger, T. C."],["dc.contributor.author","Turkenburg, MGW"],["dc.contributor.author","Uson, I."],["dc.date.accessioned","2018-11-07T10:42:39Z"],["dc.date.available","2018-11-07T10:42:39Z"],["dc.date.issued","2003"],["dc.description.sponsorship","NIGMS NIH HHS [GM-46733, 1P50GM-62412]"],["dc.identifier.doi","10.1016/S0076-6879(03)74003-8"],["dc.identifier.isi","000188419600003"],["dc.identifier.pmid","14696368"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46855"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier"],["dc.publisher.place","Amsterdam"],["dc.relation.crisseries","Methods in Enzymology"],["dc.relation.isbn","0-12-182777-1"],["dc.relation.ispartof","Macromolecular crystallography Pt. D"],["dc.relation.ispartofseries","Methods in Enzymology; 374"],["dc.title","Automatic solution of heavy-atom substructures"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]