Purification, crystallization, and preliminary X-ray diffraction analysis of rat kidney annexin V, a calcium-dependent phospholipid-binding protein.
Year: 1990
Type: article
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.
Source: Journal of Biological Chemistry
Authors: B A Seaton, J F Head, M A Kaetzel, J R Dedman
Institution: Boston University
Language: English
Topic: S100 Proteins and Annexins
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1550249153