Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein
Research output: Contribution to journal › Journal article › Research › peer-review
The nucleotide-binding domain of the Na,K-ATPase ion pump was expressed with a His tag in Escherichia coli and purified. The soluble 24 kDa derivative consists of 214 amino-acid residues and was crystallized in the presence of NiCl(2). The crystals belong to space group F23, with unit-cell parameters a = b = c = 147.5 A, and diffract to 3.1 A. Complete data sets could be collected from native and thimerosal-treated crystals frozen in 50% sucrose. Five mercury positions were found and initial SIR phases calculated.
| Original language | English |
|---|---|
| Journal | Acta crystallographica Section D: Structural biology |
| Volume | 59 |
| Issue number | Pt 7 |
| Pages (from-to) | 1259-61 |
| Number of pages | 3 |
| ISSN | 0907-4449 |
| Publication status | Published - Jul 2003 |
- Amino Acid Sequence, Animals, Binding Sites, Cloning, Molecular, Crystallization/methods, Membrane Proteins/chemistry, Nickel, Protein Structure, Tertiary, Protein Subunits/chemistry, Sodium-Potassium-Exchanging ATPase/chemistry, Swine, Thimerosal, X-Ray Diffraction/methods
Research areas
ID: 203907079