Abstract
Crystals of the human and rabbit plasma retinol-binding proteins have been grown from solutions of polyethylene glycol 6000 and CdCl2. Two crystal forms have been observed for the human protein, while the rabbit protein has only crystallized in one form which is isomorphous with one of the human serum retinol-binding protein crystals. The crystals differ in their morphologies, but are both in space group P212121 and have similar unit cell sizes (a = 45.9, b = 53.3, c = 72.0 A and a = 45.7, b = 48.7, and c = 76.5 A). The crystals diffract to approximately 2.0 A resolution. In both cases there is 1 molecule/asymmetric unit.
Highlights
Generally of the hanging-drop vapor diffusion type
The Initial attempts to improve the quality of human serum latter proteins are 15,000-dalton polypeptides which bear no RBP crystals grown from neutralized ammonium sulfate as sequence homology toRBP[5].,theplasma previously described [9] yielded only needle-shaped crystals
Protein is able tobind retinol, retinal, and retinoic acid [6], whereas the intracellular mixtures, we observed the growth of large, thick hexagonal proteinsare specific for the alcohol (CRBP) and the acid plates (1to 1.5 mm across the face of the plate, 0.25 to 0.6 (CRABP) formsof the vitamin [7,8]
Summary
Generally of the hanging-drop vapor diffusion type. Various metal salts, in concentrations ranging from 1 q M to 10 mM, were added to solutions of protein in buffered ammonium sulfate or polyethylene glycol 6000. A single human serum RBP crystal was mounted on aStoe synthesized in hepatocytes [1, 2]. The unit cell parameters for the other crystal forms of RBP from human serum, as well as those for the crystals of the rabbit serum protein, were determined from precession photographs.
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