1kme

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(New page: 200px<br /><applet load="1kme" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kme, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1kme.gif|left|200px]]<br /><applet load="1kme" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kme.gif|left|200px]]<br /><applet load="1kme" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kme, resolution 2.00&Aring;" />
caption="1kme, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF BACTERIORHODOPSIN CRYSTALLIZED FROM BICELLES'''<br />
'''CRYSTAL STRUCTURE OF BACTERIORHODOPSIN CRYSTALLIZED FROM BICELLES'''<br />
==Overview==
==Overview==
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Obtaining crystals of membrane proteins that diffract to high resolution, remains a major stumbling block in structure determination. Here we, present a new method for crystallizing membrane proteins from a bicelle, forming lipid/detergent mixture. The method is flexible and simple to use., As a test case, bacteriorhodopsin (bR) from Halobacterium salinarum was, crystallized from a bicellar solution, yielding a new bR crystal form. The, crystals belong to space group P2(1) with unit cell dimensions of a=45.0, A, b=108.9 A, c=55.9 A, beta=113.58 degrees and a dimeric asymmetric unit., The structure was solved by molecular replacement and refined at 2.0 A, resolution. In all previous bR structures the protein is organized as a, parallel trimer, but in the crystals grown from bicelles, the individual, bR subunits are arranged in an antiparallel fashion.
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Obtaining crystals of membrane proteins that diffract to high resolution remains a major stumbling block in structure determination. Here we present a new method for crystallizing membrane proteins from a bicelle forming lipid/detergent mixture. The method is flexible and simple to use. As a test case, bacteriorhodopsin (bR) from Halobacterium salinarum was crystallized from a bicellar solution, yielding a new bR crystal form. The crystals belong to space group P2(1) with unit cell dimensions of a=45.0 A, b=108.9 A, c=55.9 A, beta=113.58 degrees and a dimeric asymmetric unit. The structure was solved by molecular replacement and refined at 2.0 A resolution. In all previous bR structures the protein is organized as a parallel trimer, but in the crystals grown from bicelles, the individual bR subunits are arranged in an antiparallel fashion.
==About this Structure==
==About this Structure==
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1KME is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with GLC, RET and SQU as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KME OCA].
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1KME is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=RET:'>RET</scene> and <scene name='pdbligand=SQU:'>SQU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KME OCA].
==Reference==
==Reference==
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[[Category: Halobacterium salinarum]]
[[Category: Halobacterium salinarum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bowie, J.U.]]
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[[Category: Bowie, J U.]]
[[Category: Faham, S.]]
[[Category: Faham, S.]]
[[Category: GLC]]
[[Category: GLC]]
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[[Category: membrane protein]]
[[Category: membrane protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:21:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:43 2008''

Revision as of 11:35, 21 February 2008


1kme, resolution 2.00Å

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CRYSTAL STRUCTURE OF BACTERIORHODOPSIN CRYSTALLIZED FROM BICELLES

Overview

Obtaining crystals of membrane proteins that diffract to high resolution remains a major stumbling block in structure determination. Here we present a new method for crystallizing membrane proteins from a bicelle forming lipid/detergent mixture. The method is flexible and simple to use. As a test case, bacteriorhodopsin (bR) from Halobacterium salinarum was crystallized from a bicellar solution, yielding a new bR crystal form. The crystals belong to space group P2(1) with unit cell dimensions of a=45.0 A, b=108.9 A, c=55.9 A, beta=113.58 degrees and a dimeric asymmetric unit. The structure was solved by molecular replacement and refined at 2.0 A resolution. In all previous bR structures the protein is organized as a parallel trimer, but in the crystals grown from bicelles, the individual bR subunits are arranged in an antiparallel fashion.

About this Structure

1KME is a Single protein structure of sequence from Halobacterium salinarum with , and as ligands. Full crystallographic information is available from OCA.

Reference

Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure., Faham S, Bowie JU, J Mol Biol. 2002 Feb 8;316(1):1-6. PMID:11829498

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