4nfv: Difference between revisions

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'''Unreleased structure'''
==Previously de-ionized HEW lysozyme batch crystallized in 1.1 M MnCl2==
<StructureSection load='4nfv' size='340' side='right' caption='[[4nfv]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nfv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NFV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NFV FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4neb|4neb]], [[4ng1|4ng1]], [[4ng8|4ng8]], [[4ngi|4ngi]], [[4ngj|4ngj]], [[4ngk|4ngk]], [[4ngl|4ngl]], [[4ngo|4ngo]], [[4ngv|4ngv]], [[4ngw|4ngw]], [[4ngy|4ngy]], [[4ngz|4ngz]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
<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=4nfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nfv RCSB], [http://www.ebi.ac.uk/pdbsum/4nfv PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The influence of salt nature and concentration on tetragonal lysozyme chloride crystal solubility is presented for a set of mono-, di- and trivalent cations (Cs(+), Rb(+), Mn(2+), Co(2+) and Yb(3+)). The results show that cations have as strong an effect on protein solubility as anions and that they present their own particular effects as co-ions. Indeed, after decreasing at low ionic strength, lysozyme solubility increases with high concentration of polyvalent cations, probably due to co-ion binding and therefore the concomitant increase of the net charge of the protein-salt complex. These new results are discussed in order to progress in the understanding of the crystallisation process at the atomic level.


The entry 4nfv is ON HOLD  until Paper Publication
Strong and specific effects of cations on lysozyme chloride solubility.,Benas P, Legrand L, Ries-Kautt M Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 1):1582-7. Epub 2002, Sep 26. PMID:12351866<ref>PMID:12351866</ref>


Authors: Benas, P., Legrand, L., Ries-Kautt, M.
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Previously de-ionized HEW lysozyme batch crystallized in 1.1 M MnCl2
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Benas, P.]]
[[Category: Legrand, L.]]
[[Category: Ries-Kautt, M.]]
[[Category: Esi-mass spectrometry]]
[[Category: Hofmeister series]]
[[Category: Hydrolase]]
[[Category: Protein cation interaction]]
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