Surface electrostatic potential: (A) Trimmer of RSFP shown in orientation with the 3-fold axis in the figure plane; (B) zoom of the binding cleft.

<p>Surface electrostatic potential: (A) Trimmer of RSFP shown in orientation with the 3-fold axis in the figure plane; (B) zoom of the binding cleft.</p

The emission spectra of rhodamine B (RB; 1.225×10⁻³ g L⁻¹) and RSFP protein (0.081 g L⁻¹).

<p>The emission spectra of rhodamine B (RB; 1.225×10⁻³ g L⁻¹) and RSFP protein (0.081 g L⁻¹).</p

Alignment of <i>apo</i> RSFP form (blue) and its complex with RB (deep pink): (A) general view of monomers, (B) enlargement of loop I19-L30 with shown difference in location of S22, Y25 and F61 caused by interaction with phosphate ion and RB molecule.

<p>Alignment of <i>apo</i> RSFP form (blue) and its complex with RB (deep pink): (A) general view of monomers, (B) enlargement of loop I19-L30 with shown difference in location of S22, Y25 and F61 caused by interaction with phosphate ion and RB molecule.</p

The UV-VIS absorption spectra of rhodamine B (brown and orange lines) in the presence of the different concentration of <i>E. coli</i> proteins, respectively, and the UV-VIS absorption spectrum of rhodamine B in the absence of <i>E. coli</i> proteins (pink line).

<p>The concentration of <i>E. coli</i> proteins in the first analyzed sample (brown line) was twice higher than the concentration of <i>E. coli</i> proteins (0.023 g L⁻¹) in the second one (orange line), respectively. The concentration of RB (3.5×10⁻⁴ g L⁻¹) was the same in the all assayed samples.</p

The pink fluorescence assay: RB in PBS buffer (A), PBS buffer (B), RB+RSFP in PBS buffer (C), RSFP in PBS buffer (D), RB+<i>E. coli</i> LMG194/pBADRSFP cell lysate in PBS buffer (E), <i>E. coli</i> LMG194/pBADRSFP cell lysate in PBS buffer (F), RB+<i>E. coli</i> LMG194/pBADMycHisA cell lysate in PBS buffer (G), and <i>E. coli</i> LMG194/pBADMycHisA cell lysate in PBS buffer (H).

<p>The pink fluorescence assay: RB in PBS buffer (A), PBS buffer (B), RB+RSFP in PBS buffer (C), RSFP in PBS buffer (D), RB+<i>E. coli</i> LMG194/pBADRSFP cell lysate in PBS buffer (E), <i>E. coli</i> LMG194/pBADRSFP cell lysate in PBS buffer (F), RB+<i>E. coli</i> LMG194/pBADMycHisA cell lysate in PBS buffer (G), and <i>E. coli</i> LMG194/pBADMycHisA cell lysate in PBS buffer (H).</p

The UV-VIS absorption spectra of rhodamine B (green and blue lines) in the presence of the different concentration of RSFP protein, respectively, and the UV-VIS absorption spectrum of rhodamine B in the absence of RSFP protein (pink line).

<p>The concentration of RSFP protein in the first analyzed sample (green line) was twice higher than the concentration of RSFP protein (0.023 g L⁻¹) in the second one (blue line), respectively. The concentration of RB (3.5×10⁻⁴ g L⁻¹) was the same in the all assayed samples.</p

X-ray data collection and crystal structure refinement statistics.

1<p>Values in parentheses correspond to the last resolution shell.</p>2<p>R_int = ∑_h∑_j | I_hj−h> |/∑_h∑_j I_hj, where I_hj is the intensity of observation j of reflection h.</p>3<p>R = ∑_h | | F_o|−| F_c| |/∑_h | F_o| for all reflections, where F_o and F_c are observed and calculated structure factors, respectively.</p><p>R_free is calculated analogously for the test reflections, randomly selected and excluded from the refinement.</p

Cytokine production of splenocytes stimulated with TLA <i>in vitro</i>.

<p>Spleens were excised on day 83 (after vaccination and infection) and single cell suspensions were prepared and stimulated with TLA <i>in vitro</i>. Results represent data two independent experiments. Data are expressed as mean ±SEM.</p><p>^acomparison to sham-vaccinated and infected mice</p><p>^a<i>p</i> < 0.05</p><p>^aa<i>p</i> < 0.01</p><p>^aaa<i>p</i> < 0.001.</p><p>^bcomparison to TLA-vaccinated and infected mice</p><p>^b<i>p</i> < 0.05</p><p>^bb<i>p</i> < 0.01.</p><p>Cytokine production of splenocytes stimulated with TLA <i>in vitro</i>.</p