Structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization

Wang, Y.-L.; Chow, S.-Y.; Lin, Y.-T.; Hsieh, Y.-C.; Lee, G.-C.; Liaw, S.-H.

doi:10.1107/S1399004714022500

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 1
Sedimentation-velocity analysis of DrTS. The enzyme concentration was 0.1 mg ml⁻¹ in 20 mM Tris–HCl pH 7.5, 100 mM NaCl. The three panels represent the optical traces (top), the residuals of the model fitting (middle) and the sedimentation-coefficient distribution (bottom). The ultracentrifugation analysis demonstrated that DrTS exists as a dimer in solution.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 12| November 2014| Pages 3144-3154

doi:10.1107/S1399004714022500

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