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New page: left|200px<br /><applet load="2aro" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aro, resolution 2.10Å" /> '''Crystal Structure Of...
 
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[[Image:2aro.gif|left|200px]]<br /><applet load="2aro" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2aro.gif|left|200px]]<br /><applet load="2aro" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2aro, resolution 2.10&Aring;" />
caption="2aro, resolution 2.10&Aring;" />
'''Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione'''<br />
'''Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione'''<br />


==Overview==
==Overview==
A H3 dimer band is produced when purified native histone octamers are run, on an SDS-PAGE gel in a beta-mercaptoethanol-free environment. To, investigate this, native histone octamer crystals, derived from chicken, erythrocytes, and of structure (H2A-H2B)-(H4-H3)-(H3'-H4')-(H2B'-H2A'), were grown in 2 M KCl, 1.35 M potassium phosphates and 250-350 microM of, the oxidising agent S-nitrosoglutathione, pH 6.9. X-ray diffraction data, were acquired to 2.10 A resolution, yielding a structure with an Rwork, value of 18.6% and an Rfree of 22.5%. The space group is P6(5), the, asymmetric unit of which contains one complete octamer. Compared to the, 1.90 A resolution, unoxidised native histone octamer structure, the, crystals show a reduction of 2.5% in the c-axis of the unit cell, and, free-energy calculations reveal that the H3-H3' dimer interface in the, latter has become thermodynamically stable, in contrast to the former., Although the inter-sulphur distance of the two H3 cysteines in the, oxidised native histone octamer has reduced to 6 A from the 7 A of the, unoxidised form, analysis of the hydrogen bonds that constitute the, (H4-H3)-(H3'-H4') tetramer indicates that the formation of a disulphide, bond in the H3-H3' dimer interface is incompatible with stable tetramer, formation. The biochemical and biophysical evidence, taken as a whole, is, indicative of crystals that have a stable H3-H3' dimer interface, possibly, extending to the interface within an isolated H3-H3' dimer, observed in, SDS-PAGE gels.
A H3 dimer band is produced when purified native histone octamers are run on an SDS-PAGE gel in a beta-mercaptoethanol-free environment. To investigate this, native histone octamer crystals, derived from chicken erythrocytes, and of structure (H2A-H2B)-(H4-H3)-(H3'-H4')-(H2B'-H2A'), were grown in 2 M KCl, 1.35 M potassium phosphates and 250-350 microM of the oxidising agent S-nitrosoglutathione, pH 6.9. X-ray diffraction data were acquired to 2.10 A resolution, yielding a structure with an Rwork value of 18.6% and an Rfree of 22.5%. The space group is P6(5), the asymmetric unit of which contains one complete octamer. Compared to the 1.90 A resolution, unoxidised native histone octamer structure, the crystals show a reduction of 2.5% in the c-axis of the unit cell, and free-energy calculations reveal that the H3-H3' dimer interface in the latter has become thermodynamically stable, in contrast to the former. Although the inter-sulphur distance of the two H3 cysteines in the oxidised native histone octamer has reduced to 6 A from the 7 A of the unoxidised form, analysis of the hydrogen bonds that constitute the (H4-H3)-(H3'-H4') tetramer indicates that the formation of a disulphide bond in the H3-H3' dimer interface is incompatible with stable tetramer formation. The biochemical and biophysical evidence, taken as a whole, is indicative of crystals that have a stable H3-H3' dimer interface, possibly extending to the interface within an isolated H3-H3' dimer, observed in SDS-PAGE gels.


==About this Structure==
==About this Structure==
2ARO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with PO4 and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ARO OCA].  
2ARO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARO OCA].  


==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Baldwin, J.P.]]
[[Category: Baldwin, J P.]]
[[Category: Lambert, S.J.]]
[[Category: Lambert, S J.]]
[[Category: Nicholson, J.M.]]
[[Category: Nicholson, J M.]]
[[Category: Reynolds, C.D.]]
[[Category: Reynolds, C D.]]
[[Category: Sodngam, S.]]
[[Category: Sodngam, S.]]
[[Category: Wood, C.M.]]
[[Category: Wood, C M.]]
[[Category: CL]]
[[Category: CL]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: oxidation]]
[[Category: oxidation]]


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