Fig. 1: Structure of LRRK1 and the inactive kinase domain of LRRK1.
From: Structure and regulation of full-length human leucine-rich repeat kinase 1
A Mass photometry mass distributions for, i) the LRRK1 monomer, and ii) the LRRK1 dimer fractions. B SEC-MALS chromatogram for the LRRK1 monomer. C Cryo-EM map and model of the LRRK1 monomer, i) map from global non-uniform refinement, ii) map from local refinement of the C-terminal RCKW domains, iii) atomic model of the LRRK1 monomer, colored according to the schematic. D Cryo-EM analysis of the LRRK1 dimer, i) cryo-EM map of the LRRK1 dimer, ii) two copies of the LRRK1 monomer fit in the LRRK1 dimer map. E The broken kinase R-Spine (RS) in the kinase domain in the LRRK1 monomer, indicating that the kinase domain is in the inactive conformation. Maps in C were generated after post-processing in deepEMhancer59, maps in D were generated after sharpening in Cryosparc.
