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. Author manuscript; available in PMC: 2012 Jan 7.
Published in final edited form as: J Mol Biol. 2010 Oct 28;405(1):65–76. doi: 10.1016/j.jmb.2010.10.004

Fig. 2.

Fig. 2

The dimeric arrangement of UvsX30–358 in the crystal asymmetric unit. (A) UvsX30–358 is colored as in Figure 1A. The ATP-binding sites are indicated by the phosphate groups (orange/red CPK), and are occluded at the dimer interface. The paired Cys316 residues at the dimer interface appear to form a partially occupied disulfide bridge (yellow CPK) in the crystal and in solution (see Figure 3). The positions of the N- and C-termini and Loops L1 and L2 are indicated. The positions of Pro322 highlighted in Figure 1C are marked with cyan asterisks. (B) Six dimers create one turn of a helical array in the P61 unit cell. Interactions between successive monomer A molecules (blue) mediate the helical filament with no contributions from monomer B (grey).