Structure of human ADAM-8 catalytic domain complexed with batimastat

Hall, T.; Shieh, H.-S.; Day, J.E.; Caspers, N.; Chrencik, J.E.; Williams, J.M.; Pegg, L.E.; Pauley, A.M.; Moon, A.F.; Krahn, J.M.; Fischer, D.H.; Kiefer, J.R.; Tomasselli, A.G.; Zack, M.D.

doi:10.1107/S1744309112015618

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
Thermal unfolding assay monitoring ADAM-8 stabilization in the presence of batimastat. The thermal unfolding behavior of ADAM-8 was analyzed at pH 7.5 in the presence (blue) or absence (red) of 1 µM batimastat. The data are presented as the negative first derivative of the change in relative fluorescence units (RFU) against temperature (T). Error bars are the standard error of the mean of three replicates. The inflection point, indicative of unfolding, is observed at 334 K in the absence of batimastat. However, in the presence of batimastat a new inflection point is observed at 355 K.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 68| Part 6| May 2012| Pages 616-621

doi:10.1107/S1744309112015618

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