Crystallization and preliminary X‐ray diffraction analysis of boar seminal plasma spermadhesin PSP‐I/PSP‐II, a heterodimer of two CUB domains

FEBS Letters

Töpfer-Petersen, Edda¹  Sanz, Libia¹  Varela, Paloma F²  Calvete, Juan J²  Romero, Antonio² 

[1] Institut für Reproduktionsmedizin, Tierärztliche Hochschule, Bünteweg 15, 30559 Hannover-Kirchrode, Germany;Instituto de Quimica-Fisica ‘Rocasolano’ C.S.I.C., Madrid, Spain

关键词: Porcine fertilization;    Boar spermadhesin PSP-I/PSP-II;    CUB domain;    Crystallization;    X-ray diffraction analysis;    PSP;    porcine seminal plasma protein;    AWN;    AQN;    proteins of the spermadhesin family denominated after their first three N-terminal amino acids in the standard one-letter code;    aSFP;    bovine acidic seminal fluid protein;    HSP;    horse seminal plasma protein;   

DOI  :  10.1016/0014-5793(96)00133-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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_1,522) and trigonal (space group P3_1,221) 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 ų/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.

【 授权许可】

Unknown