Crystallization of glycosylated and nonglycosylated phytohemagglutinin-L.
In the seeds of legume plants a class of sugar-binding proteins can be found, generally called legume lectins. In this paper we present the crystallization of phytohemagglutinin-L (PHA-L), a glycosylated lectin from the seeds of the common bean (Phaseolus vulgaris). Single PHA-L crystals were grown by vapor diffusion, using PEG as precipitant. The protein crystallizes in the monoclinic space group C2, and diffracts to a resolution of 2.7 angstroms. The unit cell parameters are a=106.3 angstroms, 121.2 angstroms, c=90.8 angstroms, and beta=93.7 degrees. The asymmetric unit probably contains one PHA-L tetramer. Crystals of a recombinant nonglycosylated form of PHA-L, grown under identical conditions, and crystals of the native PHA-L, grown in the presence of isopropanol, did not survive the mounting process.
Dao-Thi
M H
MH
Laboratorium voor Ultrastructuur, Interuniversitair Instituut voor Moleculaire Biotechnologie, Vrije Universiteit, Brussel, Belgium.
Hamelryck
T W
TW
Poortmans
F
F
Voelker
T A
TA
Chrispeels
M J
MJ
Wyns
L
L
D002240:Carbohydrate Sequence; D018360:Crystallography, X-Ray / Q000379:methods*; D004058:Diffusion; D006031:Glycosylation; D008969:Molecular Sequence Data; D010835:Phytohemagglutinins / Q000737:chemistry* / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry* / Q000378:metabolism
D010835:Phytohemagglutinins; D011994:Recombinant Proteins; C064103:phytohemagglutinin L4; D011092:Polyethylene Glycols