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Another technique, nuclear magnetic resonance, can determine structures of proteins in solution, without the need for crystals.
As an alternative, electron microscopy has been shown to be capable of resolving > 3.5 Å resolution detail in membrane proteins of modest (~ 300 kDa) size, without the need for crystals.
In contrast, single particle electron microscopy circumvents the need for crystals and although small proteins can be difficult to visualise, due to the poor signal to noise ratio, it is possible to obtain high resolution structural information on membrane proteins by this route.
The single-particle approach to cryo-EM, which emerged in the late 1970s (Frank et al., 1978; van Heel and Frank, 1981), offered the possibility of being able to determine the atomic structures of cellular machinery without the need for crystals, as required for X-ray crystallography.
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We present a new computational framework aimed at dramatically reducing time needed for crystal plasticity simulations.
Unfortunately, encapsulation within a partial micelle diminishes specific protein-to-protein contacts needed for crystal lattice formation.
The molecules are then not in their natural wet state but the need for large crystals is avoided, making these TEM techniques competitive with x-ray crystallography.
The biaxially ordered films produced by IBAD make good templates for subsequent heteroepitaxial growth of functional layers if they are appropriately lattice matched, thus eliminating the need for single crystal substrates.
Approached by a client with a serious need for a crystal-encrusted lighting source, Asylum's crew of 24 model and effect artists— a team that has tackled everything from snails to giant humans carved out from a CNC machine— divvied up the project according to respective skill sets, and began constructing the base structure to fit their custom electronics into.
An explanation for this phenomenon is not obvious and underlines the need for a crystal structure of HSL.
The recent publication of the apo-, closed-state 3D crystal structure of zebrafish (zf) P2X4.1 has not only revolutionized the P2X research field, but also highlighted the need for further crystal structures, of receptors in different activation states, so that we can gain a complete molecular understanding of ion channel function.
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