Fig. 8
From: Diverse protein assembly driven by metal and chelating amino acids with selectivity and tunability
Thermal stability and enzymatic activities of protein rods and planes. a Changes in the length of rods formed at 37 °C before and after heating at 55 °C. The optimal Ni2+ ratios for each variant are shown with asterisks. b The native enzyme activities as acetyltransferases in the reactions with acetyl coenzyme A and kanamycin before and after heating at 55 °C. The error bars for the unheated samples (black columns) in (b) indicate the standard deviations of the 11, 23, 12, 5, 4, 11, and 13 runs of kinetic measurements with the wild-type, K44Z, K44Z-rods, E13Z-rods, E13Z/K44E-rods, K337Z, and K337Z-planes, respectively. The error bars for the heated samples (red columns) indicate the standard deviations of the 10, 3, and 9 runs of the experiments with K44Z-rods, E13Z/K44E-rods, and K337Z-planes, respectively. The raw data are provided as a Source Data file.
