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[[Image:2a7b.gif|left|200px]]


{{Structure
==On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength==
|PDB= 2a7b |SIZE=350|CAPTION= <scene name='initialview01'>2a7b</scene>, resolution 1.65&Aring;
<StructureSection load='2a7b' size='340' side='right'caption='[[2a7b]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=XE:XENON'>XE</scene>
<table><tr><td colspan='2'>[[2a7b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7B FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
|GENE= Ap1g1, Adtg, Clapg1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7b OCA], [https://pdbe.org/2a7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7b RCSB], [https://www.ebi.ac.uk/pdbsum/2a7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7b ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7b OCA], [http://www.ebi.ac.uk/pdbsum/2a7b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a7b RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/AP1G1_MOUSE AP1G1_MOUSE] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
== 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/a7/2a7b_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/main_output.php?pdb_ID=2a7b ConSurf].
<div style="clear:both"></div>


'''On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength'''
==See Also==
 
*[[Adaptin 3D structures|Adaptin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Complete and highly redundant data sets were collected at different wavelengths between 0.80 and 2.65 A for a total of ten different protein and DNA model systems. The magnitude of the anomalous signal-to-noise ratio as assessed by the quotient R(anom)/R(r.i.m.) was found to be influenced by the data-collection wavelength and the nature of the anomalously scattering substructure. By utilizing simple empirical correlations, for instance between the estimated deltaF/F and the expected R(anom) or the data-collection wavelength and the expected R(r.i.m.), the wavelength at which the highest anomalous signal-to-noise ratio can be expected could be estimated even before the experiment. Almost independent of the nature of the anomalously scattering substructure and provided that no elemental X-ray absorption edge is nearby, this optimal wavelength is 2.1 A.
[[Category: Large Structures]]
 
==About this Structure==
2A7B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7B OCA].
 
==Reference==
On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength., Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16131760 16131760]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Mueller-Dieckmann C]]
[[Category: Mueller-Dieckmann, C.]]
[[Category: Panjikar S]]
[[Category: Panjikar, S.]]
[[Category: Tucker PA]]
[[Category: Tucker, P A.]]
[[Category: Weiss MS]]
[[Category: Weiss, M S.]]
[[Category: protein transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:48:48 2008''

Latest revision as of 12:11, 14 February 2024

On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection WavelengthOn the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength

Structural highlights

2a7b is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AP1G1_MOUSE Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.

Evolutionary Conservation

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

See Also

2a7b, resolution 1.65Å

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