1xji
From Proteopedia
(New page: 200px<br /><applet load="1xji" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xji, resolution 2.20Å" /> '''Bacteriorhodopsin cr...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1xji.gif|left|200px]]<br /><applet load="1xji" size=" | + | [[Image:1xji.gif|left|200px]]<br /><applet load="1xji" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xji, resolution 2.20Å" /> | caption="1xji, resolution 2.20Å" /> | ||
'''Bacteriorhodopsin crystallized in bicelles at room temperature'''<br /> | '''Bacteriorhodopsin crystallized in bicelles at room temperature'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We showed previously that high-quality crystals of bacteriorhodopsin (bR) | + | We showed previously that high-quality crystals of bacteriorhodopsin (bR) from Halobacterium salinarum can be obtained from bicelle-forming DMPC/CHAPSO mixtures at 37 degrees C. As many membrane proteins are not sufficiently stable for crystallization at this high temperature, we tested whether the bicelle method could be applied at a lower temperature. Here we show that bR can be crystallized at room temperature using two different bicelle-forming compositions: DMPC/CHAPSO and DTPC/CHAPSO. The DTPC/CHAPSO crystals grown at room temperature are essentially identical to the previous, twinned crystals: space group P21 with unit cell dimensions of a = 44.7 A, b = 108.7 A, c = 55.8 A, beta = 113.6 degrees . The room-temperature DMPC/CHAPSO crystals are untwinned, however, and belong to space group C222(1) with the following unit cell dimensions: a = 44.7 A, b = 102.5 A, c = 128.2 A. The bR protein packs into almost identical layers in the two crystal forms, but the layers stack differently. The new untwinned crystal form yielded clear density for a previously unresolved CHAPSO molecule inserted between protein subunits within the layers. The ability to grow crystals at room temperature significantly expands the applicability of bicelle crystallization. |
==About this Structure== | ==About this Structure== | ||
| - | 1XJI 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 RET, D12, D10, C14, OCT and CPS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XJI 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=RET:'>RET</scene>, <scene name='pdbligand=D12:'>D12</scene>, <scene name='pdbligand=D10:'>D10</scene>, <scene name='pdbligand=C14:'>C14</scene>, <scene name='pdbligand=OCT:'>OCT</scene> and <scene name='pdbligand=CPS:'>CPS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJI OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Boulting, G | + | [[Category: Boulting, G L.]] |
| - | [[Category: Bowie, J | + | [[Category: Bowie, J U.]] |
[[Category: Faham, S.]] | [[Category: Faham, S.]] | ||
| - | [[Category: Massey, E | + | [[Category: Massey, E A.]] |
[[Category: Yang, D.]] | [[Category: Yang, D.]] | ||
[[Category: Yohannan, S.]] | [[Category: Yohannan, S.]] | ||
| Line 27: | Line 27: | ||
[[Category: membrane protein bacteriorhodopsin]] | [[Category: membrane protein bacteriorhodopsin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:28 2008'' |
Revision as of 13:55, 21 February 2008
|
Bacteriorhodopsin crystallized in bicelles at room temperature
Overview
We showed previously that high-quality crystals of bacteriorhodopsin (bR) from Halobacterium salinarum can be obtained from bicelle-forming DMPC/CHAPSO mixtures at 37 degrees C. As many membrane proteins are not sufficiently stable for crystallization at this high temperature, we tested whether the bicelle method could be applied at a lower temperature. Here we show that bR can be crystallized at room temperature using two different bicelle-forming compositions: DMPC/CHAPSO and DTPC/CHAPSO. The DTPC/CHAPSO crystals grown at room temperature are essentially identical to the previous, twinned crystals: space group P21 with unit cell dimensions of a = 44.7 A, b = 108.7 A, c = 55.8 A, beta = 113.6 degrees . The room-temperature DMPC/CHAPSO crystals are untwinned, however, and belong to space group C222(1) with the following unit cell dimensions: a = 44.7 A, b = 102.5 A, c = 128.2 A. The bR protein packs into almost identical layers in the two crystal forms, but the layers stack differently. The new untwinned crystal form yielded clear density for a previously unresolved CHAPSO molecule inserted between protein subunits within the layers. The ability to grow crystals at room temperature significantly expands the applicability of bicelle crystallization.
About this Structure
1XJI is a Single protein structure of sequence from Halobacterium salinarum with , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystallization of bacteriorhodopsin from bicelle formulations at room temperature., Faham S, Boulting GL, Massey EA, Yohannan S, Yang D, Bowie JU, Protein Sci. 2005 Mar;14(3):836-40. Epub 2005 Feb 2. PMID:15689517
Page seeded by OCA on Thu Feb 21 15:55:28 2008
Categories: Halobacterium salinarum | Single protein | Boulting, G L. | Bowie, J U. | Faham, S. | Massey, E A. | Yang, D. | Yohannan, S. | C14 | CPS | D10 | D12 | OCT | RET | Membrane protein bacteriorhodopsin
