View source for 5a1a


==2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor==
<SX load='5a1a' size='340' side='right' viewer='molstar' caption='[[5a1a]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5a1a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A1A FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PTQ:2-PHENYLETHYL+1-THIO-BETA-D-GALACTOPYRANOSIDE'>PTQ</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=5a1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1a OCA], [https://pdbe.org/5a1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a1a RCSB], [https://www.ebi.ac.uk/pdbsum/5a1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1a ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BGAL_ECOLI BGAL_ECOLI] 
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== Publication Abstract from PubMed ==
Cryo-electron microscopy (cryo-EM) is rapidly emerging as a powerful tool for protein structure determination at high resolution. Here, we report the structure of a complex between Escherichia coli beta-galactosidase and the cell-permeant inhibitor phenylethyl beta-d-thiogalactopyranoside (PETG), determined by cryo-EM at a resolution of ~2.2 A. Besides the PETG ligand, we identified densities in the map for ~800 water molecules and for magnesium and sodium ions. While it is likely that continued advances in detector technology may further enhance resolution, our findings demonstrate that preparation of specimens of adequate quality and intrinsic protein flexibility, rather than imaging or image processing technologies, now represent the major bottlenecks to achieving resolutions close to 2 A using single particle cryo-EM.

2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor.,Bartesaghi A, Merk A, Banerjee S, Matthies D, Wu X, Milne JL, Subramaniam S Science. 2015 May 7. pii: aab1576. PMID:25953817<ref>PMID:25953817</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5a1a" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galactosidase 3D structures|Galactosidase 3D structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Banerjee S]]
[[Category: Bartesaghi A]]
[[Category: Matthies D]]
[[Category: Merk A]]
[[Category: Milne J]]
[[Category: Subramaniam S]]
[[Category: Wu X]]