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      X-ray diffraction studies on merohedrally twinned Δ1–62NtNBCe1-A crystals of the sodium/bicarbonate cotransporter

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          Abstract

          A truncated mutant missing the first 62 residues of the N-terminal, cytoplasmic domain of the sodium-bicarbonate NBCe1-A cotransporter crystallizes in space group P3 1 with pseudo- P3 121 symmetry and a hemihedral twin fraction of 33.0%. Twinned fractions and twin-pair statistics over binned resolutions confirm that the calculated twin fraction is associated with hemihedral twinning and not to non-crystallographic symmetry.

          Abstract

          NBCe1-A membrane-embedded macromolecules that cotransport sodium and bicarbonate ions across the bilayer serve to maintain acid–base homeostasis throughout the body. Defects result in a number of renal and eye disorders, including type-II renal tubular acidosis and cataracts. Here, crystals of a human truncated mutant of the cytoplasmic N-terminal domain of NBCe1 (Δ1–62NtNBCe1-A) are reported that diffract X-rays to 2.4 Å resolution. The crystal symmetry of Δ1–62NtNBCe1-A is of space group P3 1 with pseudo- P3 121 symmetry and it has a hemihedral twin fraction of 33.0%. The crystals may provide insight into the pathogenic processes observed in a subset of patients with truncating and point mutations in the gene encoding NBCe1.

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          Author and article information

          Journal
          Acta Crystallogr Sect F Struct Biol Cryst Commun
          Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun
          Acta Cryst. F
          Acta Crystallographica Section F: Structural Biology and Crystallization Communications
          International Union of Crystallography
          1744-3091
          1 July 2013
          28 June 2013
          28 June 2013
          : 69
          : Pt 7 ( publisher-idID: f130700 )
          : 796-799
          Affiliations
          [a ]Department of Medicine, The George Washington University , Washington, DC 20052, USA
          [b ]Division of Renal Diseases and Hypertension, The George Washington Medical Faculty Associates , Washington, DC 20037, USA
          [c ]Department of Physiology and Biophysics, Case Western Reserve University School of Medicine , Cleveland, OH 44106, USA
          [d ]Hospital of University of Pennsylvania , Philadelphia, PA 19104, USA
          [e ]Center for Translational Science, Children’s National Medical Center , Washington, DC 20010, USA
          Author notes
          Correspondence e-mail: hgill@ 123456gwu.edu
          Article
          pu5399 ACSFCL S1744309113016710
          10.1107/S1744309113016710
          3702328
          23832211
          1f4ff03b-aa04-496c-83e7-224452f5f8b8
          © Gill et al. 2013

          This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

          History
          : 20 March 2013
          : 15 June 2013
          Categories
          Crystallization Communications

          Molecular biology
          nbce1,bicarbonate transport
          Molecular biology
          nbce1, bicarbonate transport

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