2bs7: Difference between revisions

Revision as of 16:20, 28 July 2008

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File:2bs7.png

Template:STRUCTURE 2bs7

CRYSTAL STRUCTURE OF F17B-G IN COMPLEX WITH CHITOBIOSECRYSTAL STRUCTURE OF F17B-G IN COMPLEX WITH CHITOBIOSE

Template:ABSTRACT PUBMED 16041081

About this StructureAbout this Structure

2BS7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''CRYSTAL STRUCTURE OF F17B-G IN COMPLEX WITH CHITOBIOSE'''
+===CRYSTAL STRUCTURE OF F17B-G IN COMPLEX WITH CHITOBIOSE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16041081}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16041081 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16041081}}
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 [[Category: Pathogenesis]]
 [[Category: Protein-sugar complex]]
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