 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](dw5035fig1mag.jpg)
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Figure 1
AEC pattern of the R298A mutant of SARS-CoV Mpro. The amount of protein used was 15 µl (1 mg ml−1) and the total volume of the cell was 330 µl. (a) A typical trace of the absorbance at 250 nm of the R298A mutant during an experiment at a substrate concentration of 200 µM. The symbols represent experimental data and the lines are the results fitted to the Lamm equation using the SEDFIT program (Chou et al., 2011  ; Schuck, 2000). The best-fit distribution result is shown by dashed lines in (c). (b) The absorbance at 405 nm tracing the released product (pNA) after the first hour of the same experiment. The time interval between two successive spectra, from black to cyan, is 10 min. The inset plot shows the product at different times. The line indicates the best-fit result for the initial velocity calculation. (c) The continuous c(s) distributions of the Mpro R298A mutant from the best-fit analysis of the 250 nm results. The distributions in 10 mM phosphate buffer pH 7.6 are shown by solid lines, while those in the presence of peptide substrate at 40 and 200 µM are shown as dotted and dashed lines, respectively. The two straight dashed lines indicate the positions of the monomer (M) and dimer (D). The residual bitmaps of the raw data and the best-fit results are shown as insets. (d) Plot of the initial velocities (from 405 nm results) versus substrate concentration. The line represents the best-fit results according to the Michaelis–Menten equation. |
![[Figure 1]](dw5035fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
