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dc.contributor.advisorKotwal, Girish
dc.contributor.advisorSewell, Trevor
dc.contributor.advisorSayed, Mohamed
dc.contributor.authorAdusei-Danso, Felix
dc.contributor.otherDept. of Biotechnology
dc.contributor.otherFaculty of Science
dc.date.accessioned2013-08-27T12:17:55Z
dc.date.available2007/08/30 13:54
dc.date.available2007/08/30
dc.date.available2013-08-27T12:17:55Z
dc.date.issued2006
dc.identifier.urihttp://hdl.handle.net/11394/1980
dc.descriptionMagister Scientiae - MScen_US
dc.description.abstractThis work examined the systematic approach to protein crystallization, exploring some of the techniques that have been developed to enhance the success rate of crystallization. The work was centered on two proteins; namely Vaccinia virus complement control protein (VCP) and glutamate dehydrogenase (GDH) from Bacteriodes fragilis. The crystal structures of the full lengthe native VCP and VCP bound to heparin had already been determined. In the same way, the structure of GDH from Bacteriodes fragilis is not known, even though structures of other GDHs from different organisms have been determined.en_US
dc.language.isoenen_US
dc.publisherUniversity of the Western Capeen_US
dc.subjectCrystallizationen_US
dc.subjectCrystal growthen_US
dc.titleSystematic approach to protein crystallization: emphasis on Vaccinia virus complement control protein (VCP)en_US
dc.typeThesisen_US
dc.rights.holderUniversity of the Western Capeen_US
dc.description.countrySouth Africa


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