Hauptseite > Publikationsdatenbank > Improving the accuracy of macromolecular structure refinement at 7 Å resolution > print

001     111909
005     20200402205949.0
024 7 _ |2 pmid
|a pmid:22681901
024 7 _ |2 pmc
|a pmc:PMC3380535
024 7 _ |2 DOI
|a 10.1016/j.str.2012.04.020
024 7 _ |2 WOS
|a WOS:000305094500004
037 _ _ |a PreJuSER-111909
041 _ _ |a eng
082 _ _ |a 570
100 1 _ |0 P:(DE-HGF)0
|a Brunger, A.T.
|b 0
245 _ _ |a Improving the accuracy of macromolecular structure refinement at 7 Å resolution
260 _ _ |a London [u.a.]
|b Elsevier Science
|c 2012
300 _ _ |a 957 - 966
336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a article
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440 _ 0 |0 26723
|a Structure
|v 20
|y 6
500 _ _ |a Record converted from VDB: 16.11.2012
520 _ _ |a In X-ray crystallography, molecular replacement and subsequent refinement is challenging at low resolution. We compared refinement methods using synchrotron diffraction data of photosystem I at 7.4 Å resolution, starting from different initial models with increasing deviations from the known high-resolution structure. Standard refinement spoiled the initial models, moving them further away from the true structure and leading to high R(free)-values. In contrast, DEN refinement improved even the most distant starting model as judged by R(free), atomic root-mean-square differences to the true structure, significance of features not included in the initial model, and connectivity of electron density. The best protocol was DEN refinement with initial segmented rigid-body refinement. For the most distant initial model, the fraction of atoms within 2 Å of the true structure improved from 24% to 60%. We also found a significant correlation between R(free) values and the accuracy of the model, suggesting that R(free) is useful even at low resolution.
536 _ _ |0 G:(DE-Juel1)FUEK409
|2 G:(DE-HGF)
|a Funktion und Dysfunktion des Nervensystems
|c P33
|x 0
536 _ _ |0 G:(DE-Juel1)FUEK505
|a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
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588 _ _ |a Dataset connected to Pubmed
650 _ 2 |2 MeSH
|a Bacterial Proteins: chemistry
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Photosystem I Protein Complex: chemistry
650 _ 2 |2 MeSH
|a Protein Structure, Secondary
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Software
650 _ 2 |2 MeSH
|a Structural Homology, Protein
650 _ 7 |0 0
|2 NLM Chemicals
|a Bacterial Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Photosystem I Protein Complex
700 1 _ |0 P:(DE-HGF)0
|a Adams, P.D.
|b 1
700 1 _ |0 P:(DE-HGF)0
|a Fromme, P.
|b 2
700 1 _ |0 P:(DE-HGF)0
|a Fromme, R.
|b 3
700 1 _ |0 P:(DE-HGF)0
|a Levitt, M.
|b 4
700 1 _ |0 P:(DE-Juel1)132018
|a Schröder, G.F.
|b 5
|u FZJ
773 _ _ |0 PERI:(DE-600)2031189-8
|a 10.1016/j.str.2012.04.020
|g Vol. 20, p. 957 - 966
|p 957 - 966
|q 20<957 - 966
|t Structure
|v 20
|x 0969-2126
|y 2012
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3380535
909 C O |o oai:juser.fz-juelich.de:111909
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914 1 _ |y 2012
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