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Crystallization and preliminary X-ray diffraction studies of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis.

作者信息

Singleton M R, Isupov M N, Littlechild J A

机构信息

Departments of Chemistry and Biological Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, England.

出版信息

Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):702-3. doi: 10.1107/s0907444998016035.

Abstract

Pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis has been crystallized in a form suitable for X-ray diffraction from ammonium sulfate or ammonium dihydrogen orthophosphate using the vapour-phase diffusion method. Crystals from both precipitants are of the orthorhombic space group P21212 with unit-cell dimensions a = 94.06, b = 149.06, c = 73.54 A. A complete data set to 2.8 A resolution has been collected from crystals grown from ammonium sulfate.

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