“I had the honour of working with Alexey, Mavrx’s COO, throughout 2016. Alexey brought a rare combination of skills to Mavrx, particularly suited to earlier stage start-ups. He is very technically literate and always willing to understand the basics of the ever-changing landscape of technologies adopted in the tech sector, whilst keeping both eyes on the business’s goals and processes, so he was often the voice of reason, or frequently pointed toward the path of least resistance; both are critical to success. Alexey exuded positive and supportive leadership of the whole team, as well as being one of the hardest working people I’ve ever met. I would not hesitate to recommend Alexey for similar roles in future.”
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A core-weighted fitting method for docking atomic structures into low-resolution maps: Application to cryo-electron microscopy
Journal of Structural Biology
Abstract
Cryo-electron microscopy of “single particles” is a powerful method to analyze structures of large macromolecular assemblies that are not amenable to investigation by traditional X-ray crystallographic methods. A key step in these studies is to obtain atomic interpretations of multiprotein complexes by fitting atomic structures of individual components into maps obtained from electron microscopic data. Here, we report the use of a “core-weighting” method, combined with a…Abstract
Cryo-electron microscopy of “single particles” is a powerful method to analyze structures of large macromolecular assemblies that are not amenable to investigation by traditional X-ray crystallographic methods. A key step in these studies is to obtain atomic interpretations of multiprotein complexes by fitting atomic structures of individual components into maps obtained from electron microscopic data. Here, we report the use of a “core-weighting” method, combined with a grid-threading Monte Carlo (GTMC) approach for this purpose. The “core” of an individual structure is defined to represent the part where the density distribution is least likely to be altered by other components that comprise the macromolecular assembly of interest. The performance of the method has been evaluated by its ability to determine the correct fit of (i) the α-chain of the T-cell receptor variable domain into a simulated map of the αβ complex at resolutions between 5 and 40 Å, and (ii) the E2 catalytic domain of the pyruvate dehydrogenase into an experimentally determined map, at 14 Å resolution, of the icosahedral complex formed by 60 copies of this enzyme. Using the X-ray structures of the two test cases as references, we demonstrate that, in contrast to more traditional methods, the combination of the core-weighting method and the grid-threading Monte Carlo approach can identify the correct fit reliably and rapidly from the low-resolution maps that are typical of structures determined with the use of single-particle electron microscopy.Other authors -
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