2hmq

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(New page: 200px<br /><applet load="2hmq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hmq, resolution 1.66&Aring;" /> '''THE STRUCTURES OF ME...)
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[[Image:2hmq.gif|left|200px]]<br /><applet load="2hmq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2hmq, resolution 1.66&Aring;" />
caption="2hmq, resolution 1.66&Aring;" />
'''THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION'''<br />
'''THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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The crystallographic refinement of met and azidomet hemerythrin has been, carried out at 1.66 A resolution in an attempt to characterize precisely, the binuclear iron center in this protein. Restrained least-squares, refinement has produced molecular models giving R-values of 18.9% for met, (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet, hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein, structure in each derivative is very similar to that of myohemerythrin., The mu-oxo bridged iron center differs between the two forms. The complex, in met hemerythrin is asymmetric with the bridging oxygen closer to one of, the iron atoms while the complex in azidomet hemerythrin is symmetric., After investigations of the effects of correlation in the refinement, we, believe this difference between the two complexes is associated with, chemical differences and is not a refinement artefact.
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The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact.
==About this Structure==
==About this Structure==
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2HMQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum] with ACT and FEO as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entries 1HMQ, 1HMM and 1HMN. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HMQ OCA].
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2HMQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=FEO:'>FEO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entries 1HMQ, 1HMM and 1HMN. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMQ OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Themiste dyscritum]]
[[Category: Themiste dyscritum]]
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[[Category: Holmes, M.A.]]
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[[Category: Holmes, M A.]]
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[[Category: Stenkamp, R.E.]]
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[[Category: Stenkamp, R E.]]
[[Category: ACT]]
[[Category: ACT]]
[[Category: FEO]]
[[Category: FEO]]
[[Category: oxygen transport]]
[[Category: oxygen transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:51:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:26 2008''

Revision as of 15:43, 21 February 2008

Image:2hmq.gif

2hmq, resolution 1.66Å

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THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION

Overview

The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact.

About this Structure

2HMQ is a Single protein structure of sequence from Themiste dyscritum with and as ligands. This structure supersedes the now removed PDB entries 1HMQ, 1HMM and 1HMN. Full crystallographic information is available from OCA.

Reference

Structures of met and azidomet hemerythrin at 1.66 A resolution., Holmes MA, Stenkamp RE, J Mol Biol. 1991 Aug 5;220(3):723-37. PMID:1870128

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