Purification, crystallization, and preliminary X-ray diffraction analysis of rat kidney annexin V, a calcium-dependent phospholipid-binding protein.

نویسندگان

  • B A Seaton
  • J F Head
  • M A Kaetzel
  • J R Dedman
چکیده

We have purified annexin V, a monomeric 35-kDa protein, from rat kidney using calcium-dependent phospholipid chromatography. The identity of annexin V was confirmed by immunoblot analysis using monospecific anti-annexin V antibody. Large single crystals of annexin V in the presence of calcium have been grown from ammonium sulfate under a variety of conditions, with an optimum pH range of 7.5-8.0. The crystals diffract to at least 2.2 A Bragg spacing and are stable to x-rays. Preliminary crystallographic analysis reveals the space group to be R3, with hexagonal cell dimensions of a = b = 156.8 A and c = 36.9 A, and there is one molecule/asymmetric unit.

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 265 8  شماره 

صفحات  -

تاریخ انتشار 1990