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Protein Science, Vol 6, Issue 9 2028-2030, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Crystallization and preliminary X-ray crystallographic properties of Hsc20, a J-motif co-chaperone protein from Escherichia coli

J. R. CUPP-VICKERY and L. E. VICKERY
Department of Physiology and Biophysics, University of California, Irvine, California 92697

Hsc20 is a 20-kDa auxiliary protein that functions with the molecular chaperone Hsc66 in Escherichia coli. Crystals of Hsc20 suitable for X-ray diffraction analysis were grown using the hanging drop vapor diffusion technique in polyethylene glycol 400 containing dioxane as an additive to slow growth. The crystals are monoclinic and belong to the space group C2 with unit cell dimensions a = 125.4 A, b = 71.9 A, c = 68.8 A, and {beta} = 97.0{deg}. The crystals diffract to a minimum d-spacing of ~2.5 A resolution, and a native data set was collected to 2.7 A. The results of a self-rotation function analysis revealed threefold symmetry, suggesting three molecules of Hsc20 in the asymmetric unit and, hence, 12 molecules in the unit cell; this corresponds to a V(m) value of 2.6 A(3)/Da and a solvent content of ~53% in the crystals. Structure determination by isomorphous replacement is in progress.
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