ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Ypd1p, a 167-residue protein from Saccharomyces cerevisiae, plays a key role in osmosensing phosphorelay signal transduction. It forms part of a multistep phosphorelay system which also includes Sln1p hybrid histidine kinase and two response regulators, Ssk1p and Skn7p. It has been overexpressed in soluble form in Escherichia coli with a His6-tag at its C-terminus. The recombinant protein has been crystallized at room temperature using ammonium sulfate and lithium sulfate as precipitants. Native diffraction data have been collected to 2.3 Å using synchrotron radiation. The crystals are triclinic, belonging to the space group P1, with unit-cell parameters a = 65.78, b = 66.74, c = 65.75 Å, α = 106.60, β = 106.48, γ = 115.53°. The asymmetric unit contains four molecules of the monomeric recombinant Ypd1p, with a corresponding Vm of 2.75 Å3 Da−1 and a solvent content of 55.3%.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444999004059
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