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Figure 5
Comparison of the structures of BcGH3 from in situ and cryo-cooling data. (a) A ribbon diagram of the presumably active site of the BcGH3 structure from in situ data. Most residues lining the active site are drawn in stick format. Magenta mesh shows 2Fo − Fc electron-density map contoured at 1σ. Only one water molecule drawn as a small sphere is assigned, which forms two hydrogen bonds to protein atoms including an interaction to D336. (b) A ribbon diagram of the same active site of the BcGH3 structure from cryo-cooling data. Green mesh shows 2Fo − Fc electron-density map contoured at 1σ. A number of water molecules mediate a hydrogen-bond network. A new peak in the electron density in the active site is interpreted as a glycerol molecule with a double conformation. The glycerol molecule is colored with its C atoms in magenta.

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 22| Part 6| October 2015| Pages 1386-1395
doi:10.1107/S1600577515016598
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