2vrt: Difference between revisions

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==About this Structure==
==About this Structure==
2VRT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRT OCA].  
2VRT is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRT OCA].  


==Reference==
==Reference==
The Crystal Structure of the Escherichia coli RNase E Apoprotein and a Mechanism for RNA Degradation., Koslover DJ, Callaghan AJ, Marcaida MJ, Garman EF, Martick M, Scott WG, Luisi BF, Structure. 2008 Aug;16(8):1238-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18682225 18682225]
<ref group="xtra">PMID:18682225</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Callaghan, A J.]]
[[Category: Callaghan, A J.]]
[[Category: Garman, E F.]]
[[Category: Garman, E F.]]
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[[Category: Rnase p]]
[[Category: Rnase p]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 20 11:25:55 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 15:47:46 2009''

Revision as of 16:47, 16 February 2009

File:2vrt.png

Template:STRUCTURE 2vrt

CRYSTAL STRUCTURE OF E. COLI RNASE E POSSESSING M1 RNA FRAGMENTS- CATALYTIC DOMAINCRYSTAL STRUCTURE OF E. COLI RNASE E POSSESSING M1 RNA FRAGMENTS- CATALYTIC DOMAIN

Template:ABSTRACT PUBMED 18682225

About this StructureAbout this Structure

2VRT is a 8 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Koslover DJ, Callaghan AJ, Marcaida MJ, Garman EF, Martick M, Scott WG, Luisi BF. The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation. Structure. 2008 Aug 6;16(8):1238-44. PMID:18682225 doi:10.1016/j.str.2008.04.017

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