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We then launched crystallization trials for the variants in complex with dHax3 box DNA element.
Open image in new window Figure 2 Structures of dHax3 variants in complex with their respective target DNA elements.
In the following we shall describe a promising design for a family-study to find rare high risk variants in complex diseases used in our ongoing studies.
These data are now being used to understand the role of rare variants in complex traits and to advance the goals of precision medicine.
In an effort to elucidate the molecular mechanisms involved in enhanced activity, we carried out molecular dynamics simulations of ten MBL variants in complex with a cefotaxime intermediate.
We then present fifteen crystal structures of engineered dHax3 variants in complex with target DNA molecules, which elucidate the structural basis for the recognition of bases adenine (A) and guanine (G) by reported or uncharacterized TALE codes.
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Here, we present the high-resolution crystal structures of the three SpCas9 variants in complexes with a single-guide RNA and its altered PAM-containing, partially double-stranded DNA targets.
The functional alteration underlying this modifying effect has not been clearly elucidated, but based on accumulation of non-synonymous variants in complexes I and III, instability of supercomplexes has been originally hypothesized [4], [6].
The structure of this heterodimeric variant, in complex with substrate/product, was obtained at 1.85 Å resolution.
Fig. 2 Structure of the HLA-B*57 01 HLA-B*57 01complex with abacavariantpresented in complexd peptide P1 (colored in yellowithDB code = 3VRI.
We report here the crystal structures of a Rabex-5 variant in complex with the dimeric Rabaptin-5C21 Rabaptin-5C2122) and in complex with Rabaptin-5C212 and Rab5.
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