Home > Publications database > Physical Detwinning of Hemihedrally Twinned Hexagonal Crystals of Bacteriorhdopsin > print

001     40230
005     20200402205731.0
024 7 _ |2 pmid
|a pmid:15339801
024 7 _ |2 pmc
|a pmc:PMC1304826
024 7 _ |2 DOI
|a 10.1529/biophysj.104.046573
024 7 _ |2 WOS
|a WOS:000224732500061
037 _ _ |a PreJuSER-40230
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biophysics
100 1 _ |a Efremov, R.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB4616
245 _ _ |a Physical Detwinning of Hemihedrally Twinned Hexagonal Crystals of Bacteriorhdopsin
260 _ _ |a New York, NY
|b Rockefeller Univ. Press
|c 2004
300 _ _ |a 3608 - 3613
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 |a Biophysical Journal
|x 0006-3495
|0 882
|v 87
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Hexagonal crystals of the membrane protein bacteriorhodopsin of space group P6 3 grown in lipidic cubic phase are twinned hemihedrally. It was shown that slow changes of salt concentration in the mother liquor lead to a split of crystals so that the split parts preserved high diffraction quality. Analysis of diffraction data from split crystals by Yeates statistic and Britton plot showed that the split parts are free of twinning. It is concluded that crystals of bacteriorhodopsin are composed of several macroscopic twinning domains with sizes comparable to the original crystal. The appearance of twinning domains during crystal growth and the mechanism of splitting are discussed.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK255
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Bacteriorhodopsins: analysis
650 _ 2 |2 MeSH
|a Bacteriorhodopsins: chemistry
650 _ 2 |2 MeSH
|a Bacteriorhodopsins: ultrastructure
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Computer Simulation
650 _ 2 |2 MeSH
|a Crystallization: methods
650 _ 2 |2 MeSH
|a Crystallography: methods
650 _ 2 |2 MeSH
|a Models, Chemical
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Multiprotein Complexes: chemistry
650 _ 2 |2 MeSH
|a Multiprotein Complexes: ultrastructure
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 7 |0 0
|2 NLM Chemicals
|a Multiprotein Complexes
650 _ 7 |0 53026-44-1
|2 NLM Chemicals
|a Bacteriorhodopsins
650 _ 7 |a J
|2 WoSType
700 1 _ |a Moukhametzianov, R.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB8633
700 1 _ |a Büldt, G.
|b 2
|u FZJ
|0 P:(DE-Juel1)131957
700 1 _ |a Gordeliy, V. I.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB482
773 _ _ |a 10.1529/biophysj.104.046573
|g Vol. 87, p. 3608 - 3613
|p 3608 - 3613
|q 87<3608 - 3613
|0 PERI:(DE-600)1477214-0
|t Biophysical journal
|v 87
|y 2004
|x 0006-3495
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1304826
909 C O |o oai:juser.fz-juelich.de:40230
|p VDB
913 1 _ |k L01
|v Neurowissenschaften
|l Funktion und Dysfunktion des Nervensystems
|b Leben
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|x 0
914 1 _ |a Nachtrag
|y 2004
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
|x 0
970 _ _ |a VDB:(DE-Juel1)53486
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a UNRESTRICTED
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981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106

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