The Mycobacterium tuberculosisvapBC15 locus encodes a toxin–antitoxin complex. VapC‐15 is a toxin and possesses ribonuclease activity and VapB‐15 is an antitoxin which both binds and inhibits the VapC‐15 toxin. In this study, vapBC15 genes were cloned and co‐expressed in Escherichia coli. The complex was purified to homogeneity by affinity and size‐exclusion chromatography. The VapBC‐15 complex was crystallized using the sitting‐drop vapour‐diffusion technique. The crystals diffracted to 2.6 Å resolution and belonged to space group P212121, with unit‐cell parameters a = 85.63, b = 139.09, c = 148.86 Å. The self‐rotation function combined with Matthews coefficient and solvent‐content calculations suggests the presence of either six or eight molecules of the complex in the asymmetric unit.