Surface topography of the p3 and p6 annexin V crystal forms determined by atomic force microscopy.
Annexin V is a member of a family of structurally homologous proteins sharing the ability to bind to negatively charged phospholipid membranes in a Ca(2+)-dependent manner. The structure of the soluble form of annexin V has been solved by X-ray crystallography, while electron crystallography of two-dimensional (2D) crystals has been used to reveal the structure of its membrane-bound form. Two 2D crystal forms of annexin V have been reported to date, with either p6 or p3 symmetry. Atomic force microscopy has previously been used to investigate the growth and the topography of the p6 crystal form on supported phospholipid bilayers (Reviakine et al., 1998). The surface structure of the second crystal form, p3, is presented in this study, along with an improved topographic map of the p6 crystal form. The observed topography is correlated with the structure determined by X-ray crystallography.
Reviakine
I
I
Department of Biophysical Chemistry, GBB, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Bergsma-Schutter
W
W
Mazères-Dubut
C
C
Govorukhina
N
N
Brisson
A
A
D000818:Animals; D017304:Annexin A5 / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D007091:Image Processing, Computer-Assisted; D008051:Lipid Bilayers / Q000737:chemistry; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D051381:Rats
D017304:Annexin A5; D008051:Lipid Bilayers