Skip to main content
. 2019 Jan 25;116(7):2545–2550. doi: 10.1073/pnas.1811360116

Fig. 1.

Fig. 1.

KRAS169Q61H structure analysis using new crystallization conditions. KRAS169Q61H protein was crystallized with bound GTP-analog GppNHp. (A) Surface representation of the asymmetric unit containing the six KRAS169Q61H proteins in different colors with different chains, labeled A–F. (B) Ribbon representation of KRAS169Q61H showing an overlay of the six chains, of the asymmetric unit. The switch regions of five proteins (B–F) are identical (depicted in dark gray), and one (chain A) has a stabilized switch I and switch II (depicted in blue) due to interactions with neighboring protein molecules in the crystal lattice. Residue H61 and GppNHp are indicated and one Mg atom (shown as a magenta sphere) was identified per chain. C and D show ribbon representation overlays of the KRAS169Q61H (chain A) structure with KRAS188G12V (C, switch I and switch II depicted in green) and KRAS188G12D (D, switch I and switch II depicted in brown), highlighting structural conservation across RAS mutations.