Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding domain of flocculin, a cell-adhesion molecule from Saccharomyces carlsbergensis.
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.
Groes
Magnus
M
Carlsberg Laboratory, Department of Chemistry, Gamle Carlsberg Vej 10, DK-2500 Valby, Denmark.
Teilum
Kaare
K
Olesen
Kjeld
K
Poulsen
Flemming M
FM
Henriksen
Anette
A
D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004271:DNA, Fungal; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008358:Mannose / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012440:Saccharomyces / Q000737:chemistry*
D004271:DNA, Fungal; D005656:Fungal Proteins; D008358:Mannose