@article {1806,
	title = {Crystallization and preliminary x-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture},
	journal = {Protein Science},
	volume = {6},
	number = {3},
	year = {1997},
	note = {<p>ISI Document Delivery No.: WM740 Times Cited: 7 Cited Reference Count: 22 Dias, JM Carvalho, AL Kolln, I Calvete, JJ TopferPetersen, E Varela, PF Romero, A Urbanke, C Romao, MJ CAMBRIDGE UNIV PRESS NEW YORK</p>
},
	pages = {725-727},
	abstract = {<p>{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 degrees 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 Angstrom resolution and belong to space group P2(1)2(1)2, with cell parameters a = 52.4 Angstrom</p>
},
	keywords = {acidic seminal fluid protein analytical ultracentrifugation aSFP bovine seminal plasma crystallization CUB domain spermadhesin protein family X-ray diffraction analysis FLUID PROTEIN BOAR SPERMADHESINS ZONA-PELLUCIDA LOCALIZATION AWN-1},
	author = {Dias, JM and Carvalho, AL and Kolln, I. and Calvete, JJ and TopferPetersen, E. and Varela, P. F. and Romero, A. and Urbanke, C. and Romao, MJ}
}
