Abstract
Elucidation of the 3-D molecular structure of actin has been a challenge to protein crystallo-graphers and electron microscopists ever since the pivotal role of this 43-kDa protein in muscle contraction - and later in cellular motility and cytoskeletal architecture - has been recognized. In its functional form actin is polymerized into filaments (F-actin) which are made of two linear strands of actin subunits helically twisted around each other with a pitch of about 72 nm and an axial stagger of 2.75 nm. In most in vivo situations F-actin is complexed with stoichiometric amounts of accessory proteins - e.g. tropomyosin, troponin, crosslinking or capping proteins - via specific binding sites the actin molecule has for these proteins. While ultimately one would like to reveal a near-atomic resolution model of the actin filament, as a first step towards this goal one would be quite happy to obtain a high resolution electron density map of the actin molecule which, in turn, requires the availability of large and well ordered 3-D crystals.
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