Dataset.

Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) bound to the C-terminal homology (CTH) segment of the phosphatase LYP (PTPN22) (PDB entry 7AAM)

Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/310798
Digital.CSIC. Repositorio Institucional del CSIC
  • Manso, José A.
  • Alcón, Pablo
  • Bayón, Yolanda
  • Alonso, Andrés
  • Pereda, José M. de
Download of the data available on the publisher platform., Diffraction images of a crystal of the F-BAR domain of human PSTPIP1 (residues 1-289, Uniprot reference O43586-1) in complex with the CTH of LYP (residues 787-807, Uniprot Q9Y2R2-1). 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 3 groups, each containing of 1800 images (0.1 degree oscillation per image), collected at three different positions of the same crystal. Crystal belongs to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.0 Å, b=72.0 Å, c=205.0 Å. The asymmetric unit contains an homodimer of the F-BAR domain bound to a LYP-CTH (~53% solvent content), which is the biological complex. Diffraction data was notably anisotropic. The lowest resolution limit was 4.05 Å in the direction b* and the highest limits were 2.11 Å and 2.10 in the directions a* and c*, respectively., Peer reviewed
 
DOI: http://hdl.handle.net/10261/310798
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/310798

HANDLE: http://hdl.handle.net/10261/310798
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/310798
 
Ver en: http://hdl.handle.net/10261/310798
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/310798

Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/310786
Dataset. 2020

DIFFRACTION IMAGES OF A CRYSTAL OF THE F-BAR DOMAIN OF PSTPIP1 (PROLINE-SERINE-THREONINE PHOSPHATASE-INTERACTING PROTEIN 1) MUTANT G258A (PDB ENTRY 7AAL)

Digital.CSIC. Repositorio Institucional del CSIC
  • Manso, José A.
  • Alcón, Pablo
  • Bayón, Yolanda
  • Alonso, Andrés
  • Pereda, José M. de
Download of the data available on the publisher platform., Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (residues 1-289), mutant G258A. Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.9999 Å wavelength and a PILATUS3 6M detector. The dataset consists of 2400 images (0.15 degree oscillation per image). Crystals belong to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.19 Å, b=73.02 Å, c=205.25 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 2.92 Å in the direction b* and the highest limits were 1.97 Å and 2.09 in the directions a* and c*, respectively., Peer reviewed




Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/310796
Dataset. 2020

DIFFRACTION IMAGES OF A CRYSTAL OF THE F-BAR DOMAIN OF PSTPIP1 (PROLINE-SERINE-THREONINE PHOSPHATASE-INTERACTING PROTEIN 1) (PDB ENTRY 7AAN)

Digital.CSIC. Repositorio Institucional del CSIC
  • Manso, José A.
  • Alcón, Pablo
  • Bayón, Yolanda
  • Alonso, Andrés
  • Pereda, José M. de
Download of the data available on the publisher platform., 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., Peer reviewed




Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/310798
Dataset. 2020

DIFFRACTION IMAGES OF A CRYSTAL OF THE F-BAR DOMAIN OF PSTPIP1 (PROLINE-SERINE-THREONINE PHOSPHATASE-INTERACTING PROTEIN 1) BOUND TO THE C-TERMINAL HOMOLOGY (CTH) SEGMENT OF THE PHOSPHATASE LYP (PTPN22) (PDB ENTRY 7AAM)

Digital.CSIC. Repositorio Institucional del CSIC
  • Manso, José A.
  • Alcón, Pablo
  • Bayón, Yolanda
  • Alonso, Andrés
  • Pereda, José M. de
Download of the data available on the publisher platform., Diffraction images of a crystal of the F-BAR domain of human PSTPIP1 (residues 1-289, Uniprot reference O43586-1) in complex with the CTH of LYP (residues 787-807, Uniprot Q9Y2R2-1). 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 3 groups, each containing of 1800 images (0.1 degree oscillation per image), collected at three different positions of the same crystal. Crystal belongs to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.0 Å, b=72.0 Å, c=205.0 Å. The asymmetric unit contains an homodimer of the F-BAR domain bound to a LYP-CTH (~53% solvent content), which is the biological complex. Diffraction data was notably anisotropic. The lowest resolution limit was 4.05 Å in the direction b* and the highest limits were 2.11 Å and 2.10 in the directions a* and c*, respectively., Peer reviewed




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