 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](mv5092fig1mag.jpg)
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Figure 1
Overall structures of the observed conformations of CaM. (a) Electron density at EF-hand 2 of the non-bent monomer of crystal form 2. The Sr atom is shown in green and the 2Fo − Fc electron density is shown in cyan at a contour level of 1σ. The Fo − Fc electron density at 4.0σ when Ca was refined at the position of the Sr atom is shown in magenta. (b) The two monomers in crystal form 2 coloured by temperature factor. (c) The canonical monomer, with a straight central helix, from crystal form 2 is shown in light blue, the bent monomer from crystal form 1 in shown in green and the bent monomer from crystal form 2 is shown in magenta. The structures were superimposed based on the residue range 68–78, i.e. between the N-terminal lobe and the site of bending. (d) A temperature-factor plot of the four CaM molecules in the current crystal forms. Straight and bent conformations of crystal form 1 are shown in black and green, respectively, and straight and bent conformations of crystal form 2 are shown in blue and magenta, respectively. (e) A comparison of the conformation of the straight helix (light blue), the bent monomer from crystal form 1 (green) and the original CaM structure with a small bend at Asp80 (yellow). It is clear that the bending is more pronounced in crystal form 1 than in the original CaM structure. For clarity, the view is rotated 180° about the y axis compared with that in (c). |
![[Figure 1]](mv5092fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
