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From a pool of monoclonal antibodies, we selected one such candidate (A4D11) with high affinity for tBclA, a truncated version of the <jats:italic>B. anthracis<\/jats:italic> exosporium protein BclA. Kinetic analysis utilising both standard and kinetic titration on a Biacore biosensor indicated antibody affinities in the 300 pM range for recombinant tBclA, and the A4D11 antibody was also re\u2010formatted into scFv configuration with no loss of affinity. However, assays against <jats:italic>B. anthracis<\/jats:italic> and related <jats:italic>Bacilli<\/jats:italic> species showed limited binding of intact spores as well as significant cross\u2010reactivity between species. These results were rationalized by determination of the three\u2010dimensional crystallographic structure of the scFv\u2010tBclA complex. A4D11 binds the side of the tBclA trimer, contacting a face of the antigen normally packed against adjacent trimers within the exosporium structure; this inter\u2010spore interface is highly conserved between <jats:italic>Bacilli<\/jats:italic> species. Our results indicate the difficulty of generating a high\u2010affinity antibody to differentiate between the highly conserved spore structures of closely related species, but suggest the possibility of future structure\u2010based antibody design for this difficult target. 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