Abstract
Regucalcin is a novel calcium ion (Ca(2+)) binding protein that does not contain an EF-hand motif as a Ca(2+)-binding domain and has been demonstrated to play a multi-functional role in many cell types. Human liver regucalcin, consisting of 299 amino-acid residues, was overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method in the presence of polyethylene glycol 4000 as a precipitant. A native crystal diffracted to 2.8 A with synchrotron radiation and belongs to space group P2(1), with unit-cell parameters a = 64.87, b = 52.52, c = 86.38 A, beta = 99.86 degrees . Two molecules most probably exist in the asymmetric unit, corresponding to V(M) = 2.2 A(3) Da(-1). Heavy-atom derivative data were collected and the Pb derivative showed one high-occupancy site per molecule.
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