Raw Diffraction Images Of Lysophosphatidic Acid Receptor Lpa6
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LPA<sub>6</sub> 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 LPA<sub>6</sub> and T4 lysozyme fused within the intracellular loop 3 of LPA<sub>6</sub>. 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 P2<sub>1</sub>2<sub>1</sub>2<sub>1</sub> 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.



