Published August 17, 2017 | Version v1

Raw diffraction images of lysophosphatidic acid receptor LPA6

  • 1. Department of Biological Sciences, Graduate School of Science, The University of Tokyo
  • 2. RIKEN SPring-8 Center

Description

LPA6 is a class A G protein-coupled receptor which recognizes lysophosphatidic acid, a lipid mediator, as its ligand. The crystallization construct consists of zebrafish lysophosphatidic acid receptor LPA6 and T4 lysozyme fused within the intracellular loop 3 of LPA6. The crystals were obtained within the lipidic cubic phase. No synthetic chemical compounds were added for the crystallization.

397 small-wedge (4° or 6°/crystal) datasets collected from loop-harvested microcrystals using EIGER X 9M detector at a wavelength of 1 Å on BL32XU, SPring-8. The crystals belonged to space group P212121 with unit cell parameters a=55.9, b=65.0, c=160.7 Å.

241 datasets were merged at 3.2 Å resolution in the published result (Taniguchi et al. Nature 2017; PDB code: 5XSZ) using KAMO; see processing note https://github.com/keitaroyam/yamtbx/wiki/Processing-LPA6-data-(5XSZ)

NOTE

  • flatfield correction was not applied to the images and you need to apply it using the correction table saved in master.h5 files.

  • master.h5 files were modified; see https://github.com/keitaroyam/yamtbx/blob/master/doc/eiger-en.md

  • Most frames have lipid rings and some have ice rings.

Files

Files (26.4 GB)

Name Size
md5:63624fbe3382b5cfb9eeb5271c271c90
8.4 GB Download
md5:b75fbdbb89088a67dfaa3bddfcfd17a2
8.4 GB Download
md5:0b59b685e30a2ab0c18c238fb0865fca
9.7 GB Download

Additional details

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