Fig. 2

Optimization of the CatIB strategy by excision of the linker region. CatIB formation was evaluated by a SDS-PAGE analysis and b FIB formation efficiency for TDoT-YFP and TDoT-mCherry (Data taken from [25]) without linker (dark blue bars) compared to TDoT-L-YFP (Data taken from [25]) and TDoT-L-mCherry with linker (light blue bars). After cell disruption, the crude cell extract (CCE) was separated by centrifugation into the soluble protein containing supernatant (SN) and the insoluble FIB-containing pellet (P) fraction. Sample preparation for SDS-PAGE analysis and determination of the FIB formation efficiency was carried out as described in Fig. 1. a SDS-PAGE analysis of the respective protein fractions: CCE, SN, and P. The molecular mass of the target fusion proteins is indicated by arrows (TDoT-YFP: 33.1 kDa, TDoT-mCherry: 32.7 kDa). b FIB formation efficiency quantified as the fluorescence in P fractions expressed relative to the fluorescence of the CCE (set to 100%). The complete datasets illustrating the distribution of fluorescence in the CCE, SN and P fractions can be found in Additional file 1: Figure S3. Error bars correspond to the standard deviation of the mean derived from at least three biological replicates