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

✍ Scribed by Joao M. Dias; Ana L. Carvalho; Ingo Kolln; Juan J. Calvete; Edda Topfer-Petersen; Paloma F. Varela; Antonio Romero; Claus Urbanke; Maria J. Romao

Publisher: Cold Spring Harbor Laboratory Press
Year: 2008
Tongue: English
Weight: 347 KB
Volume: 6
Category: Article
ISSN: 0961-8368
DOI: 10.1002/pro.5560060323

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✦ Synopsis

Bovine acidic seminal fluid protein (aSFP) is a 1.29 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 degrees C by vapor diffusion in hanging drops, using ammonium sulfate, pH 4.7, and polyethyleneglycol 4,000 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 mm3 diffract to beyond 1.9 A resolution and belong to space group P2(1)2(1)2(1), 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 A3/Da, and analytical ultracentrifugation analysis show that aSFP is a monomeric protein.

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