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Protein Science, Vol 6, Issue 3 725-727, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Crystallization and preliminary X-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture

J. M. DIAS, A. L. CARVALHO, I. KOLLN, J. J. CALVETE, E. TOPFER-PETERSEN, P. F. VARELA, A. ROMERO, C. URBANKE and M. J. ROMAO
Instituto de Tecnologia Quimica e Biologica, Avenida da Republica, Apartado 127, 2780 Oeiras, Portugal

Bovine acidic seminal fluid protein (aSFP) is a 12.9 kDa polypeptide of the spermadhesin family built by a single CUB domain architecture. The CUB domain is an extracellular module present in 16 functionally diverse proteins. To determine the three-dimensional structure of aSFP, the protein was crystallized at 21{deg}C by vapor diffusion in hanging drops, using ammonium sulfate, pH 4.7, and polyethyleneglycol 4000 as precipitants, containing 10% dioxane to avoid the formation of clustered crystals. Elongated prismatic crystals with maximal size of 0.6 X 0.3 X 0.2 mm(3) diffract to beyond 1.9 A resolution and belong to space group P2(1)2(1)2, with cell parameters a = 52.4 A, b = 41.5 A, c = 48.2 A. There is one aSFP molecule per asymmetric unit, which corresponds to a crystal volume per unit molecular mass of 2.04 A(3)/Da, and analytical ultracentrifugation analysis show that aSFP is a monomeric protein.
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