Crystallization of Ca2+ ATPase in sarcoplasmic reticulum vesicles by phospholipase treatment.
Ca2+ ATPase molecules in sarcoplasmic reticulum, isolated from rabbit skeletal muscle, have been induced to crystallize into two-dimensional arrays by incubating the vesicles with phospholipase A2 and dialysing against dilute Tris/HCl buffer. These crystals differ in shape and size from those produced by treatment of the sarcoplasmic reticulum vesicles with Na3VO4. However, the unit-cell dimensions of both types of crystals are similar. The differences in shape and size are presumably due to differences in the mechanisms of crystal formation induced by treatment with phospholipase and Na3VO4.
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D000818:Animals; D000252:Calcium-Transporting ATPases; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D009132:Muscles / Q000201:enzymology; D010740:Phospholipases / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*
D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D000252:Calcium-Transporting ATPases