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

dc.contributor.authorSingleton, MR
dc.contributor.authorIsupov, MN
dc.contributor.authorLittlechild, JA
dc.date.accessioned2015-10-08T09:12:23Z
dc.date.issued1999-03
dc.description.abstractPyrrolidone 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.en_GB
dc.description.sponsorshipBBSRCen_GB
dc.identifier.citationVol. 55, Iss.3, pp. 702 - 703en_GB
dc.identifier.doi10.1107/S0907444998016035
dc.identifier.otherAD0035
dc.identifier.urihttp://hdl.handle.net/10871/18389
dc.language.isoenen_GB
dc.publisherInternational Union of Crystallographyen_GB
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pubmed/10089475en_GB
dc.relation.urlhttp://onlinelibrary.wiley.com/doi/10.1107/S0907444998016035/abstracten_GB
dc.rightsCopyright © 1999 International Union of Crystallographyen_GB
dc.subjectCrystallizationen_GB
dc.subjectCrystallography, X-Rayen_GB
dc.subjectProtein Conformationen_GB
dc.subjectPyroglutamyl-Peptidase Ien_GB
dc.subjectThermococcusen_GB
dc.titleCrystallization and preliminary X-ray diffraction studies of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis.en_GB
dc.typeArticleen_GB
dc.date.available2015-10-08T09:12:23Z
dc.identifier.issn0907-4449
exeter.place-of-publicationDENMARK
dc.descriptionJournal Articleen_GB
dc.descriptionResearch Support, Non-U.S. Gov'ten_GB
dc.identifier.journalActa Crystallographica Section D: Biological Crystallographyen_GB


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