title: Extreme X-ray sensitive modification of type I aldolases by blue dye ligand chromatography.
abstract: Aldolases purified by Blue dye ligand chromatography from a variety of vertebrate sources crystallize at room temperature in a habit similar to the monoclinic form of rabbit skeletal muscle aldolase. Crystals of aldolases thus purified including rabbit muscle aldolase are extremely sensitive to X-ray (Cu K alpha) radiation and shatter after short exposure to X-ray radiation (less than 5 min.). Crystals of aldolases purified by other techniques possess demonstrable diffraction patterns and are stable in the X-ray beam with lifetimes of the order of days. No clear distinction could be made on the basis of different biochemical assays between aldolases purified by Blue dye chromatography and those purified by other techniques.
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity; D004396:Coloring Agents; D010856:Columbidae; D003460:Crystallization; D005634:Fructose-Bisphosphate Aldolase / Q000302:isolation & purification / Q000528:radiation effects*; D007527:Isoenzymes / Q000302:isolation & purification / Q000528:radiation effects; D008024:Ligands; D008099:Liver / Q000201:enzymology; D009132:Muscles / Q000201:enzymology; D011817:Rabbits; D051381:Rats; D014227:Triazines; D014337:Trout; D014961:X-Ray Diffraction
chemical_list: D004396:Coloring Agents; D007527:Isoenzymes; D008024:Ligands; D014227:Triazines; C012842:Cibacron Blue F 3GA; D005634:Fructose-Bisphosphate Aldolase