The N-terminal cytoplasmic domain of the Na + -coupled HCO À 3 cotransporter NBCe1-A (NtNBCe1) has been linked with proximal renal tubular acidosis. In a previous purification study of recombinant NtNBCe1, crystal growth at a suboptimal protein concentration (<1 mg ml À1 ) yielded small single diamondshaped crystals that diffracted poorly. In the present study, by increasing the protein concentration 50-fold, the crystal size was doubled and robustness was also improved. Crystal annealing made the crystals suitable for X-ray diffraction. The crystals either belong to space group P3 1 21 or P3 1 with pseudo P3 1 21 symmetry, with unit-cell parameters a = 51.7, b = 51.7, c = 200.6 Å , = = 90, = 120 , and diffract X-rays to 3.0 Å resolution. The calculated Matthews number is 1.9 Å 3 Da À1 , with two monomers of molecular weight $83 kDa in the asymmetric unit. The molecular-replacement packing solution shows that the molecules form dimers by a domain-swapping mechanism.