Structure of the N-terminal domain of ClpC1 in complex with the antituberculosis natural product ecumicin reveals unique binding interactions

Wolf, N.M.; Lee, H.; Zagal, D.; Nam, J.-W.; Oh, D.-C.; Lee, H.; Suh, J.-W.; Pauli, G.F.; Cho, S.; Abad-Zapatero, C.

doi:10.1107/S2059798320004027

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 5
Cyclopeptide-binding analysis by SPR. The experimental binding sensorgrams were compared with two kinetic binding models, the 1:1 Langmuir and the heterogeneous ligand (multi-site) binding models, for ECU (a), RUF-I (b) and OMS-A (c) binding to ClpC1-FL. (d) The stoichiometry was calculated based on SPR responses.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 76| Part 5| May 2020| Pages 458-471

https://doi.org/10.1107/S2059798320004027

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