Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) (PDB entry 7AAN)

Resumo

Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (residues 1-289). Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.99987 Å wavelength and a PILATUS3 6M detector. The dataset consists of 3600 images (0.15 degree oscillation per image) that were collected: 2400 at one position and the other 1200 at a second site in the same crystal. Crystal belongs to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.3 Å, b=71.9 Å, c=204.6 Å. The asymmetric unit contains an homodimer of the F-BAR domain (~53% solvent content), which is the biological unit. Diffraction data was notably anisotropic. The lowest resolution limit was 4.32 Å in the direction b* and the highest limits were 2.12 Å and 2.17 in the directions a* and c*, respectively. The structure derived form these data is published in: Manso, J.A., Marcos, T., Ruiz-Martín, V. Casas J, Alcón P, Sánchez Crespo M, Bayón Y, de Pereda JM, Alonso A PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders. Cell. Mol. Life Sci. 79, 131 (2022). https://doi.org/10.1007/s00018-022-04173-w The structure is available at the PDB under the code 7AAN: https://www.ebi.ac.uk/pdbe/entry/pdb/7aan