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. Author manuscript; available in PMC: 2008 Feb 3.
Published in final edited form as: J Mol Biol. 2006 Oct 26;365(5):1446–1459. doi: 10.1016/j.jmb.2006.10.075

Figure 5.

Figure 5

Crystal packing interactions and mobility of the α-helical domain. (a) Stereo view along the crystallographic 2-fold axis of a D3 center in the crystals of the 3.0 Å structure. Each asymmetric unit in the cluster is colored uniquely. In this structure, differences in lattice packing tilt the αB/αC coiled-coil region by 7°, allowing it to form crystal contacts with a 2-fold related coiled-coil via the side chains of Gln426 and Leu430 (ball and stick models). Only residues 400-409 are missing in its helical turn. This structure eliminates the possibility of a dimer mediated by the coiled-coil in the crystalline lattice. (b) Temperature factors as a function of residue position in the 2.1 and 3.0 Å structures of Sfmoesin. The regions of the α-helical domain that contact the FERM domains are as stable as the FERM domain, while those at greater distances from the ERM domain have gradually increasing mobility. The change in crystal contacts between the two structures orders more of the αB/αC coiled-coil in the low resolution structure, but also disorders part of the αA-αB loop (residues 312-325).