Premium
Crystallization and preliminary X‐ray diffraction analysis of boar seminal plasma spermadhesin PSP‐I/PSP‐II, a heterodimer of two CUB domains
Author(s) -
Romero Antonio,
Varela Paloma F,
Sanz Libia,
Töpfer-Petersen Edda,
Calvete Juan J
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00133-0
Subject(s) - crystallography , crystallization , boar , trigonal crystal system , chemistry , hexagonal crystal system , x ray , crystal (programming language) , diffraction , covalent bond , crystal structure , materials science , anatomy , biology , physics , optics , programming language , organic chemistry , semen , computer science
Boar spermadhesin PSP‐I/PSP‐II ( M r 29 000–30 000), a non‐covalent heterodimer of two CUB domains, was crystallized in two crystal forms. Complete diffraction data sets for hexagonal (space group P6 1,5 22) and trigonal (space group P3 1,2 21) crystals have been collected up to 2.9 and 2.5 Å resolution, respectively. Cell constants of the hexagonal and trigonal crystal forms are , , and , , respectively. The calculated packing parameters ( V m ) are 2.8 and 3.2 Å 3 /Da for the hexagonal and trigonal crystal forms, respectively, indicating that, in both cases, the asymmetric unit is constituted by one PSP‐I/PSP‐II heterodimer. This paper reports the first crystals of a protein built up by a CUB domain architecture.