Crystallization and preliminary X-ray diffraction studies of the soluble 14 kDa beta-galactoside-binding lectin from bovine heart.
The soluble 14 kDa beta-galactoside-binding lectin from bovine heart, a member of the S-type lectin family, has been crystallized in a form suitable for X-ray diffraction analysis. The crystals, in the absence of a saccharide ligand, diffract beyond 2.5 A resolution. They are obtained from polyethylene glycol 6000 at pH 6.0. Crystals grow as monoclinic plates, space group P2(1), with cell dimensions: a = 35.47 A, b = 64.33 A, c = 58.78 A and beta = 91.7 degrees. The asymmetric unit contains two molecules related by a 2-fold non-crystallographic axis. Two lectin monomers in the asymmetric unit give a Vm of 2.4 A3/Da, i.e. a solvent content of approximately 50%. The complex of lectin with the saccharide ligand, N-acetyllactosamine, crystallizes in the space group P2(1)2(1)2 with cell dimensions: a = 63.55 A, b = 82.13 A and c = 62.39 A. Crystals of this complex diffract beyond 2.0 A resolution. Two complexes in the asymmetric unit lead to a Vm value of 2.8 A3/Da (57% solvent).
Bourne
Y
Y
Laboratoire de Cristallographie et de Cristallisation des Macromolécules Biologiques, Faculté de Médecine Secteur-Nord, Marseille, France.
Bolgiano
B
B
Nésa
M P
MP
Penfold
P
P
Johnson
D
D
Feizi
T
T
Cambillau
C
C
D000606:Amino Sugars / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D037161:Galectins; D006388:Hemagglutinins / Q000737:chemistry*; D008024:Ligands; D009124:Muscle Proteins / Q000737:chemistry*; D009206:Myocardium / Q000737:chemistry*
D000606:Amino Sugars; D037161:Galectins; D006388:Hemagglutinins; D008024:Ligands; D009124:Muscle Proteins; C000458:N-acetyllactosamine