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Abstract The SPECFEM3D_Cartesian code package is widely used in simulating seismic wave propagation on local and regional scales due to its computational efficiency compared with the one-chunk version of the SPECFEM3D_Globe code. In SPECFEM3D_Cartesian, the built-in meshing tool maps a spherically curved cube to a rectangular cube using the Universal Transverse Mercator projection (UTM). Meanwhile, the geodetic east, north, and up directions are assigned as the local x–y–z directions. This causes coordinate orientation issues in simulating waveform propagation in regions larger than 6° × 6° or near the Earth’s polar regions. In this study, we introduce a new code package, named Cartesian Meshing Spherical Earth (CMSE), that can accurately mesh the 3D geometry of the Earth’s surface under the Cartesian coordinate frame, while retaining the geodetic directions. To benchmark our new package, we calculate the residual amplitude of the CMSE synthetics with respect to the reference synthetics calculated by SPECFEM3D_Globe. In the regional scale simulations with an area of 1300 km × 1300 km, we find a maximum of 5% amplitude residual for the SPECFEM3D_Cartesian synthetics using the mesh generated by the CMSE, much smaller than the maximum amplitude residual of 100% for the synthetics based on its built-in meshing tool. Therefore, our new meshing tool CMSE overcomes the limitations of the internal mesher used by SPECFEM3D_Cartesian and can be used for more accurate waveform simulations in larger regions beyond one UTM zone. Furthermore, CMSE can deal with regions at the south and north poles that cannot be handled by the UTM projection. Although other external code packages can be used to mesh the curvature of the Earth, the advantage of the CMSE code is that it is open-source, easy to use, and fully integrated with SPECFEM3D_Cartesian. 

The Ras family of proteins play an important role in relaying signals from the outside to the inside of the cell. Ras proteins are attached by a fatty tail to the inner surface of the cell membrane. When activated they transmit a burst of signal that controls critical behaviors like growth, survival and movement. It has been suggested that to prevent these signals from being accidently activated, Ras molecules must group together at specialized sites within the membrane before passing on their message. However, visualizing how Ras molecules cluster together at these domains has thus far been challenging. As a result, little is known about where these sites are located and how Ras molecules come to a stop at these domains. Now, Lee et al. have combined two microscopy techniques called ‘single-particle tracking’ and ‘photoactivated localization microscopy' to track how individual molecules of activated Ras move in human cells grown in the lab. This revealed that Ras molecules quickly diffuse along the inside of the membrane until they arrive at certain locations that cause them to halt. However, computer models consisting of just the ‘fast’ and ‘immobile’ state could not correctly re-capture the way Ras molecules moved along the membrane. Lee et al. found that for these models to mimic the movement of Ras, a third ‘intermediate’ state of Ras mobility needed to be included. To investigate this further, Lee et al. created a fluorescent map that overlaid all the individual paths taken by each Ras molecule. The map showed regions in the membrane where the Ras molecules had stopped and possibly clustered together. Each of these ‘immobilization domains’ were then surrounded by an ‘intermediate domain’ where Ras molecules had begun to slow down their movement. Although the intermediate domains did not last long, they seemed to guide Ras molecules into the immobilization domains where they could cluster together with other molecules. From there, the cell constantly removed Ras molecules from these membrane domains and returned them back to their ‘fast’ diffusing state. Mutations in Ras proteins occur in around a third of all cancers, so a better understanding of their dynamics could help with future drug discovery. The methods used here could also be used to investigate the movement of other signaling molecules.