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Updated: Aug 7, 2026

Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications
Published on: October 30, 2013
Purification, crystallization and preliminary X-ray diffraction analysis of the yeast phosphorelay protein YPD1
1Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, OK 73019, USA.
Abstract:
YPD1 is a yeast osmoregulatory protein that functions in a phosphorelay signal-transduction pathway. YPD1 has been expressed in Escherichia coli, purified to homogeneity and crystallized. The crystals were obtained by hanging-drop vapor-diffusion using PEG 4000 as a precipitant. Preliminary X-ray diffraction analysis indicates that the crystals belong to tetragonal space group P43212 or P41212 with unit-cell dimensions a = b = 52.71, c = 244.02 A. X-ray data to 2.7 and 3.0 A have been collected from native crystals and a heavy-atom derivative, respectively. Positions for two Hg atoms have been located by analysis of difference Patterson maps.

