Abstract:
: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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Sygusch J,Beaudry Ddoi
10.1016/0022-2836(85)90274-8subject
Has Abstractpub_date
1985-11-05 00:00:00pages
215-7issue
1eissn
0022-2836issn
1089-8638pii
0022-2836(85)90274-8journal_volume
186pub_type
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