 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](rr5089fig4mag.jpg)
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Figure 4
Determination of the oligomeric state and structure of P60_tth in solution. (a) Size-exclusion chromatography of P60_tth and truncated mutants on a Superdex 75 column. The left panel shows the calibration curve and the right panel shows the elution profile of the different proteins. The elution volume and calculated apparent molecular weight are indicated above each peak. P60_tth is the full-length protein; in P60_cata, only the catalytic domain is present. In P60_1LysM, the N-terminal LysM domain has been deleted and in P60_2LysM the catalytic domain has been truncated. (b) Calculated molecular weight derived from SAXS data. The left panel shows the SAXS data and the table on the right compares the theoretical molecular weight calculated from the primary sequence with the apparent molecular weight established from the SAXS data. (c) Modelling of P60_tth in solution. The left plot represents the CRYSOL evaluation of the three models shown in the right panel. The plots clearly show that the model of the dimer fits the SAXS data better than the model of the monomer and that CORAL modelling of the linkers into the dimeric model further improves the fit. |
![[Figure 4]](rr5089fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
