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[[Image:1pmb.png|left|200px]]
==THE DETERMINATION OF THE CRYSTAL STRUCTURE OF RECOMBINANT PIG MYOGLOBIN BY MOLECULAR REPLACEMENT AND ITS REFINEMENT==
<StructureSection load='1pmb' size='340' side='right' caption='[[1pmb]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pmb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PMB FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pmb RCSB], [http://www.ebi.ac.uk/pdbsum/1pmb PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pm/1pmb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As part of a protein engineering study, the X-ray crystal structure of recombinant pig myoglobin, prepared and crystallized from E. coli, has been determined. Diffraction data were collected to 2.5 A spacing using a synchrotron X-ray source. The structure was solved using the molecular-replacement method and refined using least-squares minimization procedures to a crystallographic R factor of 18.5% using 14,481 reflections between 10 and 2.5 A. A preliminary comparison of the structure of pig myoglobin with other myoglobin structures is presented.


{{STRUCTURE_1pmb|  PDB=1pmb  |  SCENE=  }}
Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement.,Smerdon SJ, Oldfield TJ, Dodson EJ, Dodson GG, Hubbard RE, Wilkinson AJ Acta Crystallogr B. 1990 Jun 1;46 ( Pt 3):370-7. PMID:2383370<ref>PMID:2383370</ref>


===THE DETERMINATION OF THE CRYSTAL STRUCTURE OF RECOMBINANT PIG MYOGLOBIN BY MOLECULAR REPLACEMENT AND ITS REFINEMENT===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_2383370}}
 
==About this Structure==
[[1pmb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMB OCA].


==See Also==
==See Also==
*[[Myoglobin|Myoglobin]]
*[[Myoglobin|Myoglobin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:002383370</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Dodson, E J.]]
[[Category: Dodson, E J.]]

Revision as of 23:22, 28 September 2014

THE DETERMINATION OF THE CRYSTAL STRUCTURE OF RECOMBINANT PIG MYOGLOBIN BY MOLECULAR REPLACEMENT AND ITS REFINEMENTTHE DETERMINATION OF THE CRYSTAL STRUCTURE OF RECOMBINANT PIG MYOGLOBIN BY MOLECULAR REPLACEMENT AND ITS REFINEMENT

Structural highlights

1pmb is a 2 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

As part of a protein engineering study, the X-ray crystal structure of recombinant pig myoglobin, prepared and crystallized from E. coli, has been determined. Diffraction data were collected to 2.5 A spacing using a synchrotron X-ray source. The structure was solved using the molecular-replacement method and refined using least-squares minimization procedures to a crystallographic R factor of 18.5% using 14,481 reflections between 10 and 2.5 A. A preliminary comparison of the structure of pig myoglobin with other myoglobin structures is presented.

Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement.,Smerdon SJ, Oldfield TJ, Dodson EJ, Dodson GG, Hubbard RE, Wilkinson AJ Acta Crystallogr B. 1990 Jun 1;46 ( Pt 3):370-7. PMID:2383370[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Smerdon SJ, Oldfield TJ, Dodson EJ, Dodson GG, Hubbard RE, Wilkinson AJ. Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement. Acta Crystallogr B. 1990 Jun 1;46 ( Pt 3):370-7. PMID:2383370

1pmb, resolution 2.50Å

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