Specificity of sdAbs for <i>Bacillus</i> species spores.

<p>Intact and broken spores were passively immobilized to microtiter plates at equivalent optical densities to assess specificity of sdAbs.</p

Specificity of sdAbs for whole bacteria.

<p>Bacteria were either grown overnight as live cultures or obtained from either CRP or KPL as killed material. Equivalent optical densities were immobilized to microtiter dishes for analysis of specificity using a direct binding ELISA.</p

Affinity of sdAbs for <i>Bacillus anthracis</i> strains.

<p>Biotinylated sdAbs were tested for their ability to recognize a panel of <i>B. anthracis</i> strains from a number of geographic locations (acquired as irradiated spore preparation from NMRC).</p

Immunoblot analysis of sdAb target protein.

<p><i>B. anthracis</i> Sterne strain cell and spore lysates were separated via SDS-PAGE for immunoblotting using each of the sdAbs.</p

Amino acid alignments of sdAb families.

<p>Families were identified based on amino acid alignments and variability in the complementarity determining regions (CDRs) bracketed in red boxes. Single representatives of each family are shown here. Clones d3x, d9x, G1, H4, and C8x are members of families that are not described in this study.</p

Melting temperatures and recovery of native structure.

<p> <b>The recovery of native structure (rounds 1–3) was calculated from the total change in left and right ellipticity for each cycle of heating and cooling compared to the initial total ellipticity.</b></p

Binding kinetics for sdAbs.

a<p>KD values are calculated from kd/ka.</p><p>NA = No binding observed.</p