
Saccharomyces cerevisiae alpha-mannosidase (Ams1) is a cargo protein that is transported to the vacuole by the cytoplasm-to-vacuole targeting (Cvt) pathway during conditions of growth and by autophagy during conditions of starvation. After transport to the vacuole, Ams1 functions as a resident hydrolase. Ams1 has been overexpressed in the methylotrophic yeast Pichia pastoris, purified and crystallized in two crystal forms. Form I belongs to space group P2(1), with unit-cell parameters a = 145.7, b = 127.7, c = 164.0 A, beta = 101.5 degrees . Form II belongs to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 127.9, b = 163.7, c = 291.5 A. Diffraction data were collected from these crystals to a resolution of 3.3 A for form I and of 2.6 A for form II using synchrotron radiation.
Saccharomyces cerevisiae Proteins, Rotation, Data Collection, Statistics as Topic, Vesicular Transport Proteins, Saccharomyces cerevisiae, Crystallography, X-Ray, Pichia, Protein Transport, X-Ray Diffraction, alpha-Mannosidase, Vacuoles, Autophagy, Crystallization, Synchrotrons
Saccharomyces cerevisiae Proteins, Rotation, Data Collection, Statistics as Topic, Vesicular Transport Proteins, Saccharomyces cerevisiae, Crystallography, X-Ray, Pichia, Protein Transport, X-Ray Diffraction, alpha-Mannosidase, Vacuoles, Autophagy, Crystallization, Synchrotrons
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