Crystallization of Helix pomatia agglutinin (HPA), a protein from the edible snail.
Crystals of Helix pomatia agglutinin (HPA) have been grown by the hanging-drop technique using polyethylene glycol as the precipitant at 293 K. Over a period of one to two weeks the crystals grew to maximum dimensions of 0.10 x 0.05 x 0.02 mm. The crystals belong to space group P6(3)22, with unit-cell dimensions a = b = 63.3, c = 105. 2 A and Z = 12 identical monomers of M(r) = 13 kDa, aggregating into two 78 kDa hexameric protein molecules per unit cell, each with symmetry 32 (D(3)). The diffraction pattern extends to 3.6 A at 293 K.
Lisgarten
J N
JN
Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, England.
Chattopadhyay
T K
TK
Pitts
J E
JE
Palmer
R A
RA
Reynolds
C D
CD
Dao-Thi
M H
MH
Van Driessche
E
E
Beeckmans
S
S
D000818:Animals; D003460:Crystallization; D003461:Crystallography; D018360:Crystallography, X-Ray; D019281:Dimerization; D006372:Helix, Snails; D037102:Lectins / Q000737:chemistry*; D008958:Models, Molecular; D011092:Polyethylene Glycols / Q000494:pharmacology; D011487:Protein Conformation
C038095:Helix lectin; D037102:Lectins; D011092:Polyethylene Glycols