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          <fullName>Insights into the Rrf2 repressor family--the structure of CymR, the global cysteine regulator of Bacillus subtilis.</fullName>
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          <attribute name="source-text">CymR from B. subtilis crystallizes in several different crystal forms (see Table S1), but only the  orthorhombic form (P212121), which diffracts to the highest resolution will be described here  (Table 1). The asymmetric unit of this form contains three homodimers forming a hexamer with  32-point symmetry (Fig. S1). As the unit cell axes are nearly identical in this orthorhombic form,  the hexamer in the asymmetric unit is related to the dimer in a cubic form by its 3-fold  crystallographic axis. The dimensions and shape of the dimer in the crystal structure (modelled  sedimentation coefficient of 2.4S) are consistent with those determined in solution by analytical
ultracentrifugation</attribute>
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ultracentrifugation</attribute>
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