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001     9741
005     20200402205832.0
024 7 _ |2 pmid
|a pmid:20376006
024 7 _ |2 pmc
|a pmc:PMC2859093
024 7 _ |2 DOI
|a 10.1038/nature08892
024 7 _ |2 WOS
|a WOS:000276891100043
024 7 _ |a altmetric:534522
|2 altmetric
037 _ _ |a PreJuSER-9741
041 _ _ |a eng
082 _ _ |a 070
084 _ _ |2 WoS
|a Multidisciplinary Sciences
100 1 _ |0 P:(DE-Juel1)132018
|a Schröder, G.F.
|b 0
|u FZJ
245 _ _ |a Super-resolution biomolecular crystallography with low-resolution data
260 _ _ |a London [u.a.]
|b Nature Publising Group
|c 2010
300 _ _ |a 1218 - 1222
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 4484
|a Nature
|v 464
|x 0028-0836
500 _ _ |a We thank P. D. Adams, S. C. Harrison and T. D. Fenn for discussions. We also thank the National Science Foundation for computing resources (CNS-0619926), the National Institutes of Health for both Roadmap Grant PN2 (EY016525) and grant GM63718 to M. L., and the Deutsche Forschungsgemeinschaft (DFG) for support for G. F. S.
520 _ _ |a X-ray diffraction plays a pivotal role in the understanding of biological systems by revealing atomic structures of proteins, nucleic acids and their complexes, with much recent interest in very large assemblies like the ribosome. As crystals of such large assemblies often diffract weakly (resolution worse than 4 A), we need methods that work at such low resolution. In macromolecular assemblies, some of the components may be known at high resolution, whereas others are unknown: current refinement methods fail as they require a high-resolution starting structure for the entire complex. Determining the structure of such complexes, which are often of key biological importance, should be possible in principle as the number of independent diffraction intensities at a resolution better than 5 A generally exceeds the number of degrees of freedom. Here we introduce a method that adds specific information from known homologous structures but allows global and local deformations of these homology models. Our approach uses the observation that local protein structure tends to be conserved as sequence and function evolve. Cross-validation with R(free) (the free R-factor) determines the optimum deformation and influence of the homology model. For test cases at 3.5-5 A resolution with known structures at high resolution, our method gives significant improvements over conventional refinement in the model as monitored by coordinate accuracy, the definition of secondary structure and the quality of electron density maps. For re-refinements of a representative set of 19 low-resolution crystal structures from the Protein Data Bank, we find similar improvements. Thus, a structure derived from low-resolution diffraction data can have quality similar to a high-resolution structure. Our method is applicable to the study of weakly diffracting crystals using X-ray micro-diffraction as well as data from new X-ray light sources. Use of homology information is not restricted to X-ray crystallography and cryo-electron microscopy: as optical imaging advances to subnanometre resolution, it can use similar tools.
536 _ _ |0 G:(DE-Juel1)FUEK409
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|a Funktion und Dysfunktion des Nervensystems
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536 _ _ |0 G:(DE-Juel1)FUEK505
|2 G:(DE-HGF)
|a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|x 1
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Crystallization
650 _ 2 |2 MeSH
|a Crystallography, X-Ray: methods
650 _ 2 |2 MeSH
|a Databases, Protein
650 _ 2 |2 MeSH
|a Electrons
650 _ 2 |2 MeSH
|a Likelihood Functions
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Oligopeptides: chemistry
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Software
650 _ 2 |2 MeSH
|a Static Electricity
650 _ 7 |0 0
|2 NLM Chemicals
|a Oligopeptides
650 _ 7 |2 WoSType
|a J
700 1 _ |0 P:(DE-HGF)0
|a Levitt, M.
|b 1
700 1 _ |0 P:(DE-HGF)0
|a Brunger, A.T.
|b 2
773 _ _ |0 PERI:(DE-600)1413423-8
|a 10.1038/nature08892
|g Vol. 464, p. 1218 - 1222
|p 1218 - 1222
|q 464<1218 - 1222
|t Nature
|v 464
|x 0028-0836
|y 2010
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2859093
909 C O |o oai:juser.fz-juelich.de:9741
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913 1 _ |0 G:(DE-Juel1)FUEK505
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|l BioSoft Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences
|v Functional Macromolecules and Complexes
|x 0
914 1 _ |y 2010
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |0 I:(DE-Juel1)VDB942
|d 31.12.2010
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|l Strukturbiochemie
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980 _ _ |a journal
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981 _ _ |a I:(DE-Juel1)ICS-6-20110106

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