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



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



Acta Crystallographica Section D Biological Crystallography 55(3): 702-703



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 ANG. A complete data set to 2.8 ANG resolution has been collected from crystals grown from ammonium sulfate.

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Accession: 010401092

Download citation: RISBibTeXText

PMID: 10089475

DOI: 10.1107/s0907444998016035


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