3sbb
From Proteopedia
(Difference between revisions)
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- | + | [[Image:3sbb.jpg|left|200px]] | |
- | The | + | <!-- |
+ | The line below this paragraph, containing "STRUCTURE_3sbb", creates the "Structure Box" on the page. | ||
+ | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
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+ | {{STRUCTURE_3sbb| PDB=3sbb | SCENE= }} | ||
- | + | ===Disulphide-mediated Tetramer of T4 Lysozyme R76C/R80C by Synthetic Symmetrization=== | |
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+ | <!-- | ||
+ | The line below this paragraph, {{ABSTRACT_PUBMED_21898649}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 21898649 is the PubMed ID number. | ||
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+ | {{ABSTRACT_PUBMED_21898649}} | ||
+ | |||
+ | ==About this Structure== | ||
+ | [[3sbb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SBB OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:021898649</ref><references group="xtra"/> | ||
+ | [[Category: Enterobacteria phage t4]] | ||
+ | [[Category: Lysozyme]] | ||
+ | [[Category: Cascio, D.]] | ||
+ | [[Category: Laganowsky, A.]] | ||
+ | [[Category: Sawaya, M R.]] | ||
+ | [[Category: Soriaga, A B.]] | ||
+ | [[Category: Yeates, T O.]] | ||
+ | [[Category: Zhao, M.]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Metal-mediated synthetic symmetrization]] | ||
+ | [[Category: Synthetic symmetrization]] |
Revision as of 06:02, 21 September 2011
Disulphide-mediated Tetramer of T4 Lysozyme R76C/R80C by Synthetic Symmetrization
Template:ABSTRACT PUBMED 21898649
About this Structure
3sbb is a 1 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
- Laganowsky A, Zhao M, Soriaga AB, Sawaya MR, Cascio D, Yeates TO. An approach to crystallizing proteins by metal-mediated synthetic symmetrization. Protein Sci. 2011 Sep 6. doi: 10.1002/pro.727. PMID:21898649 doi:10.1002/pro.727