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2D crystal forms of annexin IV on lipid monolayers
Author(s) -
Newman R.H.,
Leonard K.,
Crumpton M.J.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80240-4
Subject(s) - monolayer , annexin , phospholipid , crystallography , chemistry , crystal (programming language) , electron microscope , annexin a2 , protein crystallization , biophysics , materials science , biochemistry , optics , crystallization , physics , biology , organic chemistry , cell , membrane , computer science , programming language
Two‐dimensional crystalline arrays of annexin IV were generated by interaction of the purified protein with a phospholipid monolayer. Image analysis of electron micrographs of the protein crystals, which diffracted to 3.5 nm respectively, revealed p6 and p3 symmetry. Annexin IV gave two crystal forms with unit cells of 18 × 18 nm and 28 × 28 nm. The former unit cells wax similar to a previously described form of annexin VI. The implications of those observations are discussed.