Crystallization and preliminary X-ray diffraction analysis of bovine seminal plasma PDC-109, a protein composed of two fibronectin type II domains.
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.
Romero
A
A
Instituto de Quimica-Fisica Rocasolano C.S.I.C., Madrid, Spain.
Varela
P F
PF
Töpfer-Petersen
E
E
Calvete
J J
JJ
D000818:Animals; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D005353:Fibronectins / Q000737:chemistry*; D029584:Prostatic Secretory Proteins; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012661:Semen / Q000737:chemistry*; D029589:Seminal Plasma Proteins
D005353:Fibronectins; D029584:Prostatic Secretory Proteins; D011506:Proteins; D029589:Seminal Plasma Proteins; C043076:beta-microseminoprotein