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The crystal structures of two constructs of RC1339/APRc from Rickettsia conorii, consisting of either residues 105–231 or 110–231 followed by a His tag, have been determined in three different crystal forms. As predicted, the fold of a monomer of APRc resembles one‐half of the mandatory homodimer of retroviral pepsin‐like aspartic proteases (retropepsins), but the quaternary structure of the dimer...
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