Crystallization and preliminary X-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture

João Miguel L. Dias, A. L. Carvalho, Ingo Kölln, Juan J. Calvete, Edda Töpfer-Petersen, Paloma Fernández Varela, Antonio Romero, Claus Urbanke, M J Romão

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

Bovine acidic seminal fluid protein (aSFP) is a 1.29 kDa polypeptide of the spermadhesin family built by a single CUB domain architecture. The CUB domain is an extracellular module present in 16 functionally diverse proteins. To determine the three-dimensional structure of aSFP, the protein was crystallized at 21 degrees C by vapor diffusion in hanging drops, using ammonium sulfate, pH 4.7, and polyethyleneglycol 4,000 as precipitants, containing 10% dioxane to avoid the formation of clustered crystals. Elongated prismatic crystals with maximal size of 0.6 x 0.3 x 0.2 mm3 diffract to beyond 1.9 A resolution and belong to space group P2(1)2(1)2(1), with cell parameters a = 52.4 A, b = 41.5 A, c = 48.2 A. There is one aSFP molecule per asymmetric unit, which corresponds to a crystal volume per unit molecular mass of 2.04 A3/Da, and analytical ultracentrifugation analysis show that aSFP is a monomeric protein.
Original languageEnglish
Pages (from-to)725-727
Number of pages3
JournalProtein Science
Volume6
Issue number3
DOIs
Publication statusPublished - 1997

Keywords

  • acidic seminal fluid protein
  • analytical ultracentrifugation
  • aSFP
  • bovine seminal plasma
  • crystallization
  • CUB domain
  • spermadhesin protein family
  • X-ray diffraction analysis

Fingerprint Dive into the research topics of 'Crystallization and preliminary X-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture'. Together they form a unique fingerprint.

Cite this