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Figure 4
Effect of the data-collection temperature on the B factors of Trp533 and surrounding residues in NvFdhAB. In all segments, the W active site is shown as sticks and spheres. The peptide chain is coloured by B factor (B factors were normalized for each structure independently), and 2mFoDFc electron-density maps, at 1.0 r.m.s.d., are shown as a violet mesh. (a) The SSX_FdhAB structure. (b) The Fdh_CryoSamePrep FdhAB structure.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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