AI Article Synopsis
- Glutaredoxin Grx1p from yeast was successfully crystallized both as a standalone protein and in a fusion with a His-tagged yellow fluorescent protein (rxYFP).
- A mutant version of Grx1p, which is glutathionylated and contains a C30S change, was crystallized in two distinct forms at low pH, with varying diffraction capabilities.
- In comparison, the rxYFP-Grx1p fusion crystallized at high pH, also displaying notable diffraction quality with synchrotron radiation.
Article Abstract
Glutaredoxin Grx1p from yeast was crystallized both as an independent protein and in a protein fusion with His-tagged yellow fluorescent protein (rxYFP). A glutathionylated C30S mutant of the 12 kDa Grx1p was crystallized in two different forms in PEG 4000 at low pH. These orthorhombic and monoclinic forms diffract to 2.0 A (synchrotron radiation) and 2.7 A (rotating-anode generator), respectively. In contrast, rxYFP-Grx1p formed crystals at high pH in MgSO(4) which diffract synchrotron radiation to 2.7 A.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242864 | PMC |
| http://dx.doi.org/10.1107/S1744309106031216 | DOI Listing |
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