1aac

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(New page: 200px<br /><applet load="1aac" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aac, resolution 1.31&Aring;" /> '''AMICYANIN OXIDIZED, ...)
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[[Image:1aac.gif|left|200px]]<br /><applet load="1aac" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1aac, resolution 1.31&Aring;" />
caption="1aac, resolution 1.31&Aring;" />
'''AMICYANIN OXIDIZED, 1.31 ANGSTROMS'''<br />
'''AMICYANIN OXIDIZED, 1.31 ANGSTROMS'''<br />
==Overview==
==Overview==
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High-resolution X-ray diffraction data to d(min) = 1.31 A were collected, on a Xuong-Hamlin area detector from crystals of the blue-copper protein, amicyanin, isolated from P. denitrificans. With coordinates from the, earlier 2.0 A structure determination as a starting point, simulated, annealing and restrained positional and temperature factor refinements, using the program X-PLOR resulted in a final R factor of 15.5%, based on, 21 131 unique reflections in the range 8.0-1.3 A. Comparison of the 1.31 A, structure with that at 2.0 A shows the same basic features. However, the, high-resolution electron-density maps clearly reveal additional solvent, molecules and significant discrete disorder in protein side chains and, within the solvent structure. As a consequence of modelling side-chain, disorder, several new hydrogen-bonding interactions were identified.
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High-resolution X-ray diffraction data to d(min) = 1.31 A were collected on a Xuong-Hamlin area detector from crystals of the blue-copper protein amicyanin, isolated from P. denitrificans. With coordinates from the earlier 2.0 A structure determination as a starting point, simulated annealing and restrained positional and temperature factor refinements using the program X-PLOR resulted in a final R factor of 15.5%, based on 21 131 unique reflections in the range 8.0-1.3 A. Comparison of the 1.31 A structure with that at 2.0 A shows the same basic features. However, the high-resolution electron-density maps clearly reveal additional solvent molecules and significant discrete disorder in protein side chains and within the solvent structure. As a consequence of modelling side-chain disorder, several new hydrogen-bonding interactions were identified.
==About this Structure==
==About this Structure==
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1AAC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AAC OCA].
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1AAC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AAC OCA].
==Reference==
==Reference==
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[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chen, Z.W.]]
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[[Category: Chen, Z W.]]
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[[Category: Cunane, L.M.]]
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[[Category: Cunane, L M.]]
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[[Category: Durley, R.C.E.]]
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[[Category: Durley, R C.E.]]
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[[Category: Mathews, F.S.]]
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[[Category: Mathews, F S.]]
[[Category: CU]]
[[Category: CU]]
[[Category: electron transport]]
[[Category: electron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:42:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:42:36 2008''

Revision as of 09:42, 21 February 2008


1aac, resolution 1.31Å

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AMICYANIN OXIDIZED, 1.31 ANGSTROMS

Overview

High-resolution X-ray diffraction data to d(min) = 1.31 A were collected on a Xuong-Hamlin area detector from crystals of the blue-copper protein amicyanin, isolated from P. denitrificans. With coordinates from the earlier 2.0 A structure determination as a starting point, simulated annealing and restrained positional and temperature factor refinements using the program X-PLOR resulted in a final R factor of 15.5%, based on 21 131 unique reflections in the range 8.0-1.3 A. Comparison of the 1.31 A structure with that at 2.0 A shows the same basic features. However, the high-resolution electron-density maps clearly reveal additional solvent molecules and significant discrete disorder in protein side chains and within the solvent structure. As a consequence of modelling side-chain disorder, several new hydrogen-bonding interactions were identified.

About this Structure

1AAC is a Single protein structure of sequence from Paracoccus denitrificans with as ligand. Full crystallographic information is available from OCA.

Reference

X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 A resolution., Cunane LM, Chen ZW, Durley RC, Mathews FS, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):676-86. PMID:15299631

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