Crystallization, preliminary X-ray analysis and Patterson search of a new aspartic protease isolated from human urine

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorCanduri, F.
dc.creatorTeodoro, LGVL
dc.creatorLorenzi, CCB
dc.creatorGomes, RAS
dc.creatorFontes, MRM
dc.creatorArni, R. K.
dc.creatorde Azevedo, W. F.
dc.date2014-05-20T13:49:22Z
dc.date2014-05-20T13:49:22Z
dc.date1998-10-01
dc.date.accessioned2017-04-05T21:01:06Z
dc.date.available2017-04-05T21:01:06Z
dc.identifierBiochemistry and Molecular Biology International. Marrickville: Academic Press Aust, v. 46, n. 2, p. 355-363, 1998.
dc.identifier1039-9712
dc.identifierhttp://hdl.handle.net/11449/17588
dc.identifier10.1080/15216549800203862
dc.identifierWOS:000076672000015
dc.identifierWOS000076672000015.pdf
dc.identifierhttp://dx.doi.org/10.1080/15216549800203862
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/864036
dc.descriptionAspartic protease (EC 3.4.23) make up a widely distributed class of enzymes in animals, plants, microbes and, viruses. In animals these enzymes perform diverse functions, which range from digestion of food proteins to very specific regulatory roles. In contrast the information about the well-characterized aspartic proteases, very little is known about the corresponding enzyme in urine. A new aspartic protease isolated from human urine has been crystallized and X-ray diffraction data collected to 2.45 Angstrom resolution using a synchrotron radiation source. Crystals belong to the space group P2(1)2(1)2(1) the cell parameters obtained were a=50.99, b=75.56 and c=89.90 Angstrom. Preliminary analysis revealed the presence of one molecule in the asymmetric unit. The structure was determined using the molecular replacement technique and is currently being refined using simulated annealing and conjugate gradient protocols.
dc.languageeng
dc.publisherAcademic Press Aust
dc.relationBiochemistry and Molecular Biology International
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectaspartic protease
dc.subjectCrystallography
dc.subjectdrug design
dc.subjectsynchrotron
dc.subjectX-ray analysis
dc.titleCrystallization, preliminary X-ray analysis and Patterson search of a new aspartic protease isolated from human urine
dc.typeOtro


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