Preliminary crystallographic investigation of rabbit liver aldolase.
Rabbit liver aldolase was purified by affinity elution on a CM52 ion exchanger. Crystals of rabbit liver aldolase suitable for X-ray diffraction experiments were grown from 45% saturated ammonium sulfate solution at 4 degrees C. The enzyme crystallizes in space group C222(1) having cell dimensions a = 377.02 A, b = 130.35 A, c = 80.04 A and diffracts to at least 3.5 A resolution. On the basis of a 55% solvent content there are eight aldolase tetramers in the unit cell. Rotational symmetry analysis to 6.7 A is consistent with the aldolase tetramers having a high degree of internal symmetry corresponding to point group 222. The crystallized enzyme is catalytically active.
D000818:Animals; D003461:Crystallography; D005634:Fructose-Bisphosphate Aldolase; D007527:Isoenzymes; D008099:Liver / Q000201:enzymology*; D011817:Rabbits
D007527:Isoenzymes; D005634:Fructose-Bisphosphate Aldolase