Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 62, Issue -, Pages 534-537Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309106015181
Keywords
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Funding
- NIDDK NIH HHS [R37 DK30344, K01 DK082646, R37 DK030344, F32 DK075258, 5T32 DK007259, T32 DK007259] Funding Source: Medline
- NINDS NIH HHS [R01 NS018400, R01 NS18400] Funding Source: Medline
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The N-terminal cytoplasmic domain of the Na+- coupled HCO3- 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(-1)) yielded small single diamond-shaped 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 angstrom, alpha = ss = 90, gamma = 120 degrees, and diffract X-rays to 3.0 A resolution. The calculated Matthews number is 1.9 angstrom(3) Da(-1), with two monomers of molecular weight similar to 83 kDa in the asymmetric unit. The molecular-replacement packing solution shows that the molecules form dimers by a domain-swapping mechanism.
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