Abstract
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.
Highlights
Purification, Crystallization, and Preliminary X-ray Diffraction Analysis of Rat Kidney Annexin V, a Calcium-dependent Phospholipid-binding Protein*
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 r%nge of 7.5-8.0
The calmodulin/troponin C superfamily is a well characterized group of calcium-binding proteins that coordinate the calcium ion within a helix-loop-helix domain termed an “E-F hand” by Kretsinger (1975). This structural domain is widely found in nature and provides proteins a mechanism to be regulated by changes in free calcium
Summary
The calmodulin/troponin C superfamily is a well characterized group of calcium-binding proteins that coordinate the calcium ion within a helix-loop-helix domain termed an “E-F hand” by Kretsinger (1975). In order to elucidate the mechanism by which the annexin family of proteins coordinates calcium ions and phospholipids, we have grown large single crystals of annexin V in the presence of calcium which are suitable for high resolution xray structure determination. To date, these are the only such annexin crystals that have been reported
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