Crystallization and preliminary X-ray diffraction analysis of the human dimeric S-Lac lectin (L-14-II).
The human recombinant S-Lac lectin, L-14-II, produced in an Escherichia coli expression system, has been co-crystallized in the presence of lactose by the hanging drop vapor diffusion method. The crystals grow in space group P2(1)2(1)2(1) with unit cell dimensions of a = 43.6 A, b = 57.8 A, c = 108.2 A, with a dimer in the asymmetric unit. On a conventional rotating anode the crystals diffract to at least 2.8 A resolution.
Lobsanov
Y D
YD
Department of Molecular Genetics, University of Toronto, Ontario, Canada.
Gitt
M A
MA
Leffler
H
H
Barondes
S
S
Rini
J M
JM
D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D037161:Galectins; D006388:Hemagglutinins / Q000737:chemistry*; D006801:Humans; D037102:Lectins / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D037161:Galectins; D006388:Hemagglutinins; D037102:Lectins; D011994:Recombinant Proteins