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Hydrated monoolein forms the cubic-Pn3m mesophase that has been used for in meso crystallization of membrane proteins.
To date, two detailed studies of in meso crystallization of integral membrane proteins that make use of hosting lipids, as implemented in the MS&FB group, have been reported.
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With these data in hand, it is reasonable to ask if any recommendations can be made with regard to choosing a particular MAG or set of MAGs with which to perform in meso crystallization trials.
In meso crystallization trials began with an initial reconstitution of the protein into the bilayer of the lipid mesophase.
Fortunately, in meso crystallization is highly efficient and requires very small amounts of protein and lipid.
A co-crystal structure with the natural dipeptide l-Ala- l-Phe (Ala-Phe) was obtained using the in meso crystallization method [ 16] and refined to a maximum resolution of 2.5 Å (Materials and Methods, Table 1 and Supplementary Fig S3).
We hypothesized that a shorter-chained lipid producing a thinner bilayer would facilitate the so-called in meso crystallization process.
As of this writing, 161 structure records have been reported in the PDB that are attributed to the in meso crystallization method.
Initial in meso crystallization trials were set up at 20 °C with monoolein (9.9 MAG) as the host lipid and with mPGES1* at 20 mg/mL in the presence of 2 mM GSH.
The synthesis has been made by using glycerin as a reaction medium via a quasi-solid-state crystallization of hierarchically meso-macroporous zirconosilicate precursor under the effect of the structure directing agent TPAOH.
In this paper, we review our experimental results on enhanced infiltration, adhesion, nucleation, and crystallization of biological and inorganic materials in meso- and macroporous silicon.
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