1xft: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1xft.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1xft", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1xft|  PDB=1xft  |  SCENE=  }}
'''Synchrotron X-ray Powder Diffraction Study of Hexagonal Turkey Egg-white Lysozyme'''


==Synchrotron X-ray Powder Diffraction Study of Hexagonal Turkey Egg-white Lysozyme==
<StructureSection load='1xft' size='340' side='right'caption='[[1xft]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xft]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XFT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray powder diffraction, [[Resolution|Resolution]] 3.35&#8491;</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=1xft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xft OCA], [https://pdbe.org/1xft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xft RCSB], [https://www.ebi.ac.uk/pdbsum/1xft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xft ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSC_MELGA LYSC_MELGA] 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.
== 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/xf/1xft_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=1xft ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of turkey egg-white lysozyme (TEWL) has been refined from high-resolution X-ray powder diffraction data. The sample was rapidly obtained as a polycrystalline precipitate at high protein concentration using 0.5 M NaCl solvent pH 6 and was deposited in the PDB with code 1xft. The diffraction data were collected at room temperature. Molecular replacement was shown to give a suitable starting point for refinement, illustrating that powder data can be sufficient for this approach. Crystallographic models were then refined by combined Rietveld and stereochemical restraint analysis of the powder data (d(min) = 3.35 A), resulting in the extraction of reliable lattice parameters and the refinement of the molecular conformation at room temperature. The structure is hexagonal [space group P6(1)22, unit-cell parameters a = 71.0862 (3), c = 85.0276 (5) A] with 12 symmetry-related molecules in the unit cell, in agreement with previous studies. The results of our analysis are indicative of specific amino acids being disordered at this temperature. Upon cooling, a sudden drop in the lattice parameters at approximately 250 K is observed concurrently with the freezing of the mother liquor. The observation of severe peak broadening below this temperature indicates strain effects accompanying the freezing transition, which are found to be reversible. Finally, a correlation between the unit-cell parameters and the pH of the buffer solution is evident, in a similar manner to earlier observations on HEWL.


==Overview==
Synchrotron X-ray powder diffraction study of hexagonal turkey egg-white lysozyme.,Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):423-32. Epub 2005, Mar 24. PMID:15805597<ref>PMID:15805597</ref>
The structure of turkey egg-white lysozyme (TEWL) has been refined from high-resolution X-ray powder diffraction data. The sample was rapidly obtained as a polycrystalline precipitate at high protein concentration using 0.5 M NaCl solvent pH 6 and was deposited in the PDB with code 1xft. The diffraction data were collected at room temperature. Molecular replacement was shown to give a suitable starting point for refinement, illustrating that powder data can be sufficient for this approach. Crystallographic models were then refined by combined Rietveld and stereochemical restraint analysis of the powder data (d(min) = 3.35 A), resulting in the extraction of reliable lattice parameters and the refinement of the molecular conformation at room temperature. The structure is hexagonal [space group P6(1)22, unit-cell parameters a = 71.0862 (3), c = 85.0276 (5) A] with 12 symmetry-related molecules in the unit cell, in agreement with previous studies. The results of our analysis are indicative of specific amino acids being disordered at this temperature. Upon cooling, a sudden drop in the lattice parameters at approximately 250 K is observed concurrently with the freezing of the mother liquor. The observation of severe peak broadening below this temperature indicates strain effects accompanying the freezing transition, which are found to be reversible. Finally, a correlation between the unit-cell parameters and the pH of the buffer solution is evident, in a similar manner to earlier observations on HEWL.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1XFT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFT OCA].
</div>
<div class="pdbe-citations 1xft" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Synchrotron X-ray powder diffraction study of hexagonal turkey egg-white lysozyme., Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB, Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):423-32. Epub 2005, Mar 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15805597 15805597]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
[[Category: Lysozyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
[[Category: Single protein]]
[[Category: Margiolaki I]]
[[Category: Margiolaki, I.]]
[[Category: Wright JP]]
[[Category: Wright, J P.]]
[[Category: Lysozyme]]
[[Category: Powder diffraction]]
[[Category: X-ray]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:58:32 2008''

Latest revision as of 00:39, 21 November 2024

Synchrotron X-ray Powder Diffraction Study of Hexagonal Turkey Egg-white Lysozyme

1xft, resolution 3.35Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1xft&oldid=4269397"