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[[Image:2bsb.png|left|200px]]
==E. COLI F17E-G LECTIN DOMAIN COMPLEX WITH N-ACETYLGLUCOSAMINE==
<StructureSection load='2bsb' size='340' side='right' caption='[[2bsb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bsb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BSB FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bsc|2bsc]]</td></tr>
<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=2bsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bsb RCSB], [http://www.ebi.ac.uk/pdbsum/2bsb PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Since the introduction of structural genomics, the protein has been recognized as the most important variable in crystallization. Recent strategies to modify a protein to improve crystal quality have included rationally engineered point mutations, truncations, deletions and fusions. Five naturally occurring variants, differing in 1-18 amino acids, of the 177-residue lectin domain of the F17G fimbrial adhesin were expressed and purified in identical ways. For four out of the five variants crystals were obtained, mostly in non-isomorphous space groups, with diffraction limits ranging between 2.4 and 1.1 A resolution. A comparative analysis of the crystal-packing contacts revealed that the variable amino acids are often involved in lattice contacts and a single amino-acid substitution can suffice to radically change crystal packing. A statistical approach proved reliable to estimate the compatibilities of the variant sequences with the observed crystal forms. In conclusion, natural variation, universally present within prokaryotic species, is a valuable genetic resource that can be favourably employed to enhance the crystallization success rate with considerably less effort than other strategies.


{{STRUCTURE_2bsb|  PDB=2bsb  |  SCENE=  }}
Impact of natural variation in bacterial F17G adhesins on crystallization behaviour.,Buts L, Wellens A, Van Molle I, Wyns L, Loris R, Lahmann M, Oscarson S, De Greve H, Bouckaert J Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1149-59. Epub 2005, Jul 20. PMID:16041081<ref>PMID:16041081</ref>


===E. COLI F17E-G LECTIN DOMAIN COMPLEX WITH N-ACETYLGLUCOSAMINE===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_16041081}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2bsb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSB OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:016041081</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Bouckaert, J.]]
[[Category: Bouckaert, J.]]
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