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Expression and crystallization of the yeast Hsp82 chaperone, and preliminary x‐ray diffraction studies of the amino‐terminal domain

✍ Scribed by Prodromou, Chrisostomos; Piper, Peter W.; Pearl, Laurence H.

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
592 KB
Volume
25
Category
Article
ISSN
0887-3585

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✦ Synopsis

Expression of the Saccharomyces cerevisiae Hsp82 chaperone in a pep4-3and hsc82-deficient strain of S. cerevisiae yielded over 25% of the total cell protein as intact Hsp82. Similarly, the amino-terminal domain (residues 1-220) of Hsp82 was expressed to 18% of the total cell protein. Crystals of the intact Hsp82 were readily obtained. The crystals were very fragile, suggesting a high solvent content, and diffracted to approximately 8 A.

Tetragonal bipyrimidal crystals of the aminoterminal domain of Hsp82 were readily obtained under a variety of different conditions. The crystals have primitive tetragonal space group (P422, P4,22, or its enantiomorph P%22) with unit cell dimensions of a = 75.1 A and c = 111.3 A, contain 60% by volume solvent, and diffract to 2.5 A resolution. Addition of 25% glycerol to the mother liquor gave rise to large rodshaped crystals. The crystals diffract to 2.8 A resolution, have an orthorhombic space group (P222,, P2,2,2, or P2,2,2,) with cell dimensions of a = 45.2 A, b = 115.4 A, and c = 116.9 A, and a solvent content of 58% by volume.

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