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4e3u

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[[Image:4e3u.png|left|200px]]
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==Crystal Structure of Hen Egg White Lysozyme Cryoprotected in Proline==
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<StructureSection load='4e3u' size='340' side='right' caption='[[4e3u]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4e3u]] 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=4E3U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E3U FirstGlance]. <br>
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</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=PRO:PROLINE'>PRO</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e3v|4e3v]], [[4e3w|4e3w]], [[4e3x|4e3x]]</td></tr>
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<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>
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<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=4e3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e3u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e3u RCSB], [http://www.ebi.ac.uk/pdbsum/4e3u PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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L-Proline is one of Mother Nature's cryoprotectants. Plants and yeast accumulate proline under freeze-induced stress and the use of proline in the cryopreservation of biological samples is well established. Here, it is shown that L-proline is also a useful cryoprotectant for protein crystallography. Proline was used to prepare crystals of lysozyme, xylose isomerase, histidine acid phosphatase and 1-pyrroline-5-carboxylate dehydrogenase for low-temperature data collection. The crystallization solutions in these test cases included the commonly used precipitants ammonium sulfate, sodium chloride and polyethylene glycol and spanned the pH range 4.6-8.5. Thus, proline is compatible with typical protein-crystallization formulations. The proline concentration needed for cryoprotection of these crystals is in the range 2.0-3.0 M. Complete data sets were collected from the proline-protected crystals. Proline performed as well as traditional cryoprotectants based on the diffraction resolution and data-quality statistics. The structures were refined to assess the binding of proline to these proteins. As observed with traditional cryoprotectants such as glycerol and ethylene glycol, the electron-density maps clearly showed the presence of proline molecules bound to the protein. In two cases, histidine acid phosphatase and 1-pyrroline-5-carboxylate dehydrogenase, proline binds in the active site. It is concluded that L-proline is an effective cryoprotectant for protein crystallography.
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{{STRUCTURE_4e3u| PDB=4e3u | SCENE= }}
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Proline: Mother Nature's cryoprotectant applied to protein crystallography.,Pemberton TA, Still BR, Christensen EM, Singh H, Srivastava D, Tanner JJ Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):1010-8. Epub 2012 Jul 17. PMID:22868767<ref>PMID:22868767</ref>
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===Crystal Structure of Hen Egg White Lysozyme Cryoprotected in Proline===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_22868767}}
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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==About this Structure==
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== References ==
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[[4e3u]] 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=4E3U OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:022868767</ref><references group="xtra"/>
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]

Revision as of 09:15, 11 June 2014

Crystal Structure of Hen Egg White Lysozyme Cryoprotected in Proline

4e3u, resolution 1.50Å

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