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. 1997 Jul;28(3):454-6.
doi: 10.1002/(sici)1097-0134(199707)28:3<454::aid-prot14>3.0.co;2-g.

Crystallization and preliminary X-ray diffraction analysis of bovine seminal plasma PDC-109, a protein composed of two fibronectin type II domains

A Romero  1 , P F Varela, E Töpfer-Petersen, J J Calvete
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Crystallization and preliminary X-ray diffraction analysis of bovine seminal plasma PDC-109, a protein composed of two fibronectin type II domains

A Romero et al. Proteins. 1997 Jul.

Abstract

PDC-109 is a 13 kDa glycoprotein and the major phosphorylcholine- and heparin-binding protein of bull seminal plasma. It is built by an acidic 23-residue N-terminal sequence followed by a tandem of fibronectin type II domains. Full-length PDC-109 was crystallized in complex with o-phosphorylcholine by vapor diffusion in sitting drops. Crystals grew to maximal size of 0.5 x 0.3 x 0.2 mm3, diffract x-rays beyond 2.6 A resolution, and belong to space group P321 with unit cell dimensions a = b = 93.6 A, c = 52.7 A.

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