1xso
From Proteopedia
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===THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY AT 1.5 ANGSTROMS RESOLUTION=== | ===THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY AT 1.5 ANGSTROMS RESOLUTION=== | ||
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==About this Structure== | ==About this Structure== | ||
- | + | [[1xso]] is a 2 chain structure of [[Superoxide Dismutase]] with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSO OCA]. | |
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+ | ==See Also== | ||
+ | *[[Superoxide Dismutase|Superoxide Dismutase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015299740</ref><ref group="xtra">PMID:011880627</ref><references group="xtra"/> |
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
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[[Category: Rotilio, G.]] | [[Category: Rotilio, G.]] | ||
[[Category: Wilson, K S.]] | [[Category: Wilson, K S.]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:31:22 2009'' |
Revision as of 12:55, 26 July 2012
Contents |
THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY AT 1.5 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 15299740
About this Structure
1xso is a 2 chain structure of Superoxide Dismutase with sequence from Xenopus laevis. Full crystallographic information is available from OCA.
See Also
Reference
- Djinovic Carugo K, Battistoni A, Carri MT, Polticelli F, Desideri A, Rotilio G, Coda A, Wilson KS, Bolognesi M. Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b determined by X-ray crystallography at 1.5 A resolution. Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):176-88. PMID:15299740 doi:http://dx.doi.org/10.1107/S0907444995007608
- Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099