Literature DB >> 12454478

Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding domain of flocculin, a cell-adhesion molecule from Saccharomyces carlsbergensis.

Magnus Groes1, Kaare Teilum, Kjeld Olesen, Flemming M Poulsen, Anette Henriksen.   

Abstract

The recombinant carbohydrate-binding domain of the cell-surface lectin flocculin from brewer's yeast has been identified, purified and crystallized. The expression of the protein is associated with the nutritional state of the yeast. P2(1)2(1)2(1) crystals with unit-cell parameters a = 36.5, b = 59.7, c = 83.1 A were obtained in hanging drops at 295 K using 25%(w/v) PEG 4000, 0.05 M KH(2)PO(4) as precipitant. X-ray diffraction data have been obtained to 2.6 A. The asymmetric unit contains one molecule and has a solvent content of 32%. An isomorphous PtCl(4)(2-) derivative has been obtained.

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Year:  2002        PMID: 12454478     DOI: 10.1107/s0907444902015494

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  The N-terminal domain of the Flo1 flocculation protein from Saccharomyces cerevisiae binds specifically to mannose carbohydrates.

Authors:  Katty V Y Goossens; Catherine Stassen; Ingeborg Stals; Dagmara S Donohue; Bart Devreese; Henri De Greve; Ronnie G Willaert
Journal:  Eukaryot Cell       Date:  2010-11-12

2.  The mannose-specific lectin domains of Flo1p from Saccharomyces cerevisiae and Lg-Flo1p from S. pastorianus: crystallization and preliminary X-ray diffraction analysis of the adhesin-carbohydrate complexes.

Authors:  Francesco S Ielasi; Parveen Goyal; Mike Sleutel; Alexandre Wohlkonig; Ronnie G Willaert
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-06-28
  2 in total

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