CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF BOVINE SEMINAL PLASMA PDC-109, A PROTEIN COMPOSED OF 2 FIBRONECTIN TYPE-II DOMAINS

Citation
A. Romero et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF BOVINE SEMINAL PLASMA PDC-109, A PROTEIN COMPOSED OF 2 FIBRONECTIN TYPE-II DOMAINS, Proteins, 28(3), 1997, pp. 454-456
Citations number
32
Categorie Soggetti
Biology
Journal title
ISSN journal
08873585
Volume
28
Issue
3
Year of publication
1997
Pages
454 - 456
Database
ISI
SICI code
0887-3585(1997)28:3<454:CAPDAO>2.0.ZU;2-G
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 acid ic 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 mm(3), diffract x-rays beyond 2.6 Angstrom resolution, and belong to space group P321 with unit cell dim ensions a = b = 93.6 Angstrom, c = 52.7 Angstrom. (C) 1997 Wiley-Liss, Inc.