1iua

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(New page: 200px<br /><applet load="1iua" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iua, resolution 0.80&Aring;" /> '''Ultra-high resolutio...)
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[[Image:1iua.gif|left|200px]]<br /><applet load="1iua" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1iua, resolution 0.80&Aring;" />
caption="1iua, resolution 0.80&Aring;" />
'''Ultra-high resolution structure of HiPIP from Thermochromatium tepidum'''<br />
'''Ultra-high resolution structure of HiPIP from Thermochromatium tepidum'''<br />
==Overview==
==Overview==
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Crystals of the high-potential iron-sulfur protein (HiPIP) from, Thermochromatium tepidum diffract X-rays to 0.80 A using synchrotron, radiation at 100 K. The crystal structure of this HiPIP was refined at, this ultrahigh resolution with anisotropic temperature factors for all, atoms to conventional crystallographic R factors of 0.092 and 0.101 for, F(o) &gt; 4sigma(F(o)) and all reflections, respectively. The present, structure provides a more precise picture than the previous 1.5 A, structure and allows location of the positions of most H atoms. The, structure revealed a partly hydrophobic cavity near the main hydrophobic, area and a much larger inter-cluster approach distance (23.454 A, the c, constant of the unit cell) in the crystal packing than other types of, HiPIPs. The structural features involved in the electron-transfer reaction, of HiPIP are discussed.
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Crystals of the high-potential iron-sulfur protein (HiPIP) from Thermochromatium tepidum diffract X-rays to 0.80 A using synchrotron radiation at 100 K. The crystal structure of this HiPIP was refined at this ultrahigh resolution with anisotropic temperature factors for all atoms to conventional crystallographic R factors of 0.092 and 0.101 for F(o) &gt; 4sigma(F(o)) and all reflections, respectively. The present structure provides a more precise picture than the previous 1.5 A structure and allows location of the positions of most H atoms. The structure revealed a partly hydrophobic cavity near the main hydrophobic area and a much larger inter-cluster approach distance (23.454 A, the c constant of the unit cell) in the crystal packing than other types of HiPIPs. The structural features involved in the electron-transfer reaction of HiPIP are discussed.
==About this Structure==
==About this Structure==
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1IUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermochromatium_tepidum Thermochromatium tepidum] with SO4 and SF4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IUA OCA].
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1IUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermochromatium_tepidum Thermochromatium tepidum] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUA OCA].
==Reference==
==Reference==
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[[Category: ultra-high resolution]]
[[Category: ultra-high resolution]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:40:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:41 2008''

Revision as of 11:15, 21 February 2008


1iua, resolution 0.80Å

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Ultra-high resolution structure of HiPIP from Thermochromatium tepidum

Overview

Crystals of the high-potential iron-sulfur protein (HiPIP) from Thermochromatium tepidum diffract X-rays to 0.80 A using synchrotron radiation at 100 K. The crystal structure of this HiPIP was refined at this ultrahigh resolution with anisotropic temperature factors for all atoms to conventional crystallographic R factors of 0.092 and 0.101 for F(o) > 4sigma(F(o)) and all reflections, respectively. The present structure provides a more precise picture than the previous 1.5 A structure and allows location of the positions of most H atoms. The structure revealed a partly hydrophobic cavity near the main hydrophobic area and a much larger inter-cluster approach distance (23.454 A, the c constant of the unit cell) in the crystal packing than other types of HiPIPs. The structural features involved in the electron-transfer reaction of HiPIP are discussed.

About this Structure

1IUA is a Single protein structure of sequence from Thermochromatium tepidum with and as ligands. Full crystallographic information is available from OCA.

Reference

Ultrahigh-resolution structure of high-potential iron-sulfur protein from Thermochromatium tepidum., Liu L, Nogi T, Kobayashi M, Nozawa T, Miki K, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1085-91. Epub 2002, Jun 20. PMID:12077426

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