Fig. 3: Characterization of Cry3Aa-yCD crystals. | Communications Biology

Fig. 3: Characterization of Cry3Aa-yCD crystals.

From: An engineered yeast cytosine deaminase with improved catalytic activity and stability for macrophage-mediated enzyme/prodrug therapy

Fig. 3

A Enzymatic activities of the various Cry3Aa fusion crystals were determined by monitoring the conversion of 5-FC to 5-FU. 500 nM of the fusion crystals were reacted with 1 mM of 5-FC in PBS at 37 °C, and the absorbance at 276 to 266 nm was measured at different times (n = 3). B Kinetic stability of Cry3Aa-yCD fusion crystals and its variants were determined by pre-incubating the crystals in PBS at 37 °C for different lengths of time prior to measuring their residual activity. The residual activity was normalized to the corresponding protein crystals without pre-incubation (n = 3). C Scanning electron micrographs of Cry3Aa-yCD-M100H crystals. Magnification: 10,000x. Scale bar: 5 μm. D Size distribution of the purified Cry3Aa-yCD-M100H protein crystals as measured by dynamic light scattering. E Histogram of the zeta potential of Cry3Aa-yCD-M100H crystals measured on a Malvern Zetasizer Nano ZS90.

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