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In situ crystallography as an emerging method for structure solution of membrane proteins: the case of CCR2A
Author(s) -
Cheng Robert,
Huang ChiaYing,
Hennig Michael,
Nar Herbert,
Schnapp Gisela
Publication year - 2020
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15098
Subject(s) - crystallization , in situ , chemokine receptor , g protein coupled receptor , chemistry , transmembrane protein , receptor , ligand (biochemistry) , crystallography , chemokine , computational biology , materials science , biology , biochemistry , organic chemistry
The in meso in situ serial X‐ray crystallization method (Huang et al., (2015) Acta Crystallogr D Biol Crystallogr 71 , 1238) combines lipid cubic phase crystallization, direct freezing of the crystallization droplet without handling of the crystals, and data collection in situ. Recently, this method was used to overcome the mechanical fragility of crystals which enabled the X‐ray structure determination of chemokine receptor 2A (Apel et al., (2019) Structure 27 , 427) at 2.7 Å resolution. The CCR2 structure provides the structural basis for ligand selectivity of CCR2 against chemokine receptor 5 and provides insights into the residence time of MK‐0812 analogs based on molecular dynamics simulations. These findings offer new opportunities for drug discovery targeting chemokine receptors.