2bsb
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(New page: 200px<br /> <applet load="2bsb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bsb, resolution 2.4Å" /> '''E. COLI F17E-G LECTI...)
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Revision as of 17:31, 29 October 2007
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E. COLI F17E-G LECTIN DOMAIN COMPLEX WITH N-ACETYLGLUCOSAMINE
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 ... [(full description)]
About this Structure
2BSB is a [Single protein] structure of sequence from [Escherichia coli] with NAG as [ligand]. Full crystallographic information is available from [OCA].
Reference
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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