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[[Image:1iee.jpg|left|200px]]
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{{STRUCTURE_1iee|  PDB=1iee  |  SCENE=  }}
'''STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME AT 0.94 A FROM CRYSTALS GROWN BY THE COUNTER-DIFFUSION METHOD'''


==STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME AT 0.94 A FROM CRYSTALS GROWN BY THE COUNTER-DIFFUSION METHOD==
<StructureSection load='1iee' size='340' side='right'caption='[[1iee]], [[Resolution|resolution]] 0.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iee]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IEE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.94&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iee OCA], [https://pdbe.org/1iee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iee RCSB], [https://www.ebi.ac.uk/pdbsum/1iee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iee ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
== 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/ie/1iee_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1iee ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Very high quality crystals of tetragonal hen egg-white lysozyme were grown in the Advanced Protein Crystallization Facility (APCF) on board the Space Shuttle using a modified free-interface diffusion (FID) reactor designed ad hoc to have a longer diffusion path. This design allows the performance of true counter-diffusion experiments. Crystals were obtained under the classical chemical conditions defined 50 y ago with NaCl as a crystallizing agent and acetate pH 4.5 as a buffer. Counter-diffusion crystallization allows a "physical" instead of chemical optimization of growth conditions: indeed, this method screens for the best supersaturation conditions in a single trial and yields crystals of very high quality. A complete diffraction data set was collected at atomic resolution from one of these crystals using synchrotron radiation at the DESY-EMBL beamlines. The overall R(merge) on intensities in the resolution range 31-0.94 A was 5.2% and the data were 98.9% complete. Refinement was carried out with the programs CNS and SHELX97 to a final crystallographic R factor of 12.26% for 72 390 reflections. A mean standard uncertainty in the atomic positions of 0.024 A was estimated from inversion of blocked least-squares matrices. 22 side chains show alternate conformations and the loop 59-75 adopts in the same crystal packing two conformations that were observed for either triclinic or tetragonal lysozyme in previous high-resolution studies. In addition to 255 water molecules, the crystallizing agent (one hexacoordinated sodium ion and five chloride anions) participates in the ordered lysozyme hydration shell.


==Overview==
Structure of tetragonal hen egg-white lysozyme at 0.94 A from crystals grown by the counter-diffusion method.,Sauter C, Otalora F, Gavira JA, Vidal O, Giege R, Garcia-Ruiz JM Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1119-26. Epub 2001, Jul 23. PMID:11468395<ref>PMID:11468395</ref>
Very high quality crystals of tetragonal hen egg-white lysozyme were grown in the Advanced Protein Crystallization Facility (APCF) on board the Space Shuttle using a modified free-interface diffusion (FID) reactor designed ad hoc to have a longer diffusion path. This design allows the performance of true counter-diffusion experiments. Crystals were obtained under the classical chemical conditions defined 50 y ago with NaCl as a crystallizing agent and acetate pH 4.5 as a buffer. Counter-diffusion crystallization allows a "physical" instead of chemical optimization of growth conditions: indeed, this method screens for the best supersaturation conditions in a single trial and yields crystals of very high quality. A complete diffraction data set was collected at atomic resolution from one of these crystals using synchrotron radiation at the DESY-EMBL beamlines. The overall R(merge) on intensities in the resolution range 31-0.94 A was 5.2% and the data were 98.9% complete. Refinement was carried out with the programs CNS and SHELX97 to a final crystallographic R factor of 12.26% for 72 390 reflections. A mean standard uncertainty in the atomic positions of 0.024 A was estimated from inversion of blocked least-squares matrices. 22 side chains show alternate conformations and the loop 59-75 adopts in the same crystal packing two conformations that were observed for either triclinic or tetragonal lysozyme in previous high-resolution studies. In addition to 255 water molecules, the crystallizing agent (one hexacoordinated sodium ion and five chloride anions) participates in the ordered lysozyme hydration shell.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1IEE is a [[Single protein]] structure of 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=1IEE OCA].
</div>
<div class="pdbe-citations 1iee" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of tetragonal hen egg-white lysozyme at 0.94 A from crystals grown by the counter-diffusion method., Sauter C, Otalora F, Gavira JA, Vidal O, Giege R, Garcia-Ruiz JM, Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1119-26. Epub 2001, Jul 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11468395 11468395]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Garcia-Ruiz J-M]]
[[Category: Garcia-Ruiz, J M.]]
[[Category: Gavira J-A]]
[[Category: Gavira, J A.]]
[[Category: Giege R]]
[[Category: Giege, R.]]
[[Category: Otalora F]]
[[Category: Otalora, F.]]
[[Category: Sauter C]]
[[Category: Sauter, C.]]
[[Category: Vidal O]]
[[Category: Vidal, O.]]
[[Category: 1,4-beta-n-acetylmuramidase c]]
[[Category: Hydrolase]]
[[Category: Lysozyme]]
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