 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](ek5033fig1mag.jpg)
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Figure 1
Microbiological and biochemical characterization of the proteins from the faRel2/aTfaRel2 TA operon. (a–d) In vivo toxicity neutralization assays were used to assess the effects of substitutions on FaRel2 toxicity. Serial dilutions of E. coli strains were plated on solid LB medium and scored after 16 h at 37°C uninduced (grey) and under induction conditions (blue). (e) Coomassie-stained SDS–PAGE of purified ATfaRel2 (lane 2; molecular-weight markers are shown in lane 1). (f) Coomassie-stained SDS–PAGE of the ATfaRel2–FaRel2Y128F complex (lane 2) and FaRel2Y128F (lane 3); molecular-weight markers are shown in lane 1. The migration of the band corresponding to ATfaRel2 is highlighted by a solid black triangle and that for FaRel2Y128F by an open triangle. (g) Analytical SEC of ATfaRel2, FaRel2Y128F and the ATfaRel2–FaRel2Y128F complex on a Superdex 75 Increase column in 25 mM HEPES, 300 mM NaCl, 1 mM TCEP, 2 mM MgCl2. (h) ITC titration to monitor the interaction of ATfaRel2 with its 150 bp operator region. |
![[Figure 1]](ek5033fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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