Abstract
The Plasmodium yoelii reticulocyte-binding protein Py235 has a role as an ATP/ADP sensor. The sensor domain of Py235 is called NBD94; it consists of at least three functional regions, the nucleotide-binding region (NBD94444-547), hinge region (NBD94566-663) and C-terminal coupling region (NBD94674-781), and has been proposed to link ATP/ADP binding to the interaction of Py235 with the red blood cell. Here, NBD94674-781 was cloned, expressed and purified to high purity. The monodisperse protein was crystallized by vapour diffusion. A diffraction data set was collected to 2.9 Å resolution with 97.2% completeness using a synchrotron-radiation source. The crystals belonged to space group C2, with unit-cell parameters a = 65.08, b = 82.71, c = 114.27 Å, Β = 94.72°, and contained four molecules in the asymmetric unit.
Original language | English |
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Pages (from-to) | 1631-1634 |
Number of pages | 4 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 66 |
Issue number | 12 |
DOIs | |
Publication status | Published - Dec 2010 |
Externally published | Yes |
ASJC Scopus Subject Areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics
Keywords
- ATP/ADP sensors
- malaria
- nucleotide-binding domain
- Plasmodium