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

Citation:
Dias, JM, AL Carvalho, I. Kolln, JJ Calvete, E. TopferPetersen, P. F. Varela, A. Romero, C. Urbanke, and MJ Romao. "Crystallization and preliminary x-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture." Protein Science. 6 (1997): 725-727.

Abstract:

{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

Notes:

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