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http://purl.uniprot.org/citations/16041081http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16041081http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16041081http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.org/dc/terms/identifier"doi:10.1107/s0907444905017038"xsd:string
http://purl.uniprot.org/citations/16041081http://purl.org/dc/terms/identifier"doi:10.1107/s0907444905017038"xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Wyns L."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Wyns L."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Loris R."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Loris R."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Buts L."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Buts L."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Van Molle I."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Van Molle I."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Bouckaert J."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Bouckaert J."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Oscarson S."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Oscarson S."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"De Greve H.M.J."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"De Greve H.M.J."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Lahmann M."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Lahmann M."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Wellens A."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/author"Wellens A."xsd:string
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16041081http://purl.uniprot.org/core/date"2005"xsd:gYear