Event Title
Required Modifications for the Expression and Purification of the E290K Mutant of Horse Heart Cytochrome C Peroxidase.
Presentation Type
Poster/Portfolio
Presenter Major(s)
Chemistry
Mentor Information
Cory DiCarlo
Department
Chemistry
Location
Henry Hall Atrium 89
Start Date
11-4-2012 9:00 AM
Keywords
Physical Science
Abstract
Expression of mutant horse heart cytochrome c peroxidase (HH CcP) was carried out using a recombinant bacterial expression system. Crystallization of HH CcP mutant E290K was realized with the formation of purified protein crystals. Although crystallization of this mutant was attained other mutant strains were found to be less receptive of the techniques used during the early stages of isolation. Crystal size was found to be diminutive and recrystallization for the sample will need to be performed to increase crystal dimensions for crystallography to be performed. Further development and honing of the procedures for cell cultures, protein isolation and purification was carried out through acclimatizing prior procedures to attain improved realizations of product though each stage of product collection.
Required Modifications for the Expression and Purification of the E290K Mutant of Horse Heart Cytochrome C Peroxidase.
Henry Hall Atrium 89
Expression of mutant horse heart cytochrome c peroxidase (HH CcP) was carried out using a recombinant bacterial expression system. Crystallization of HH CcP mutant E290K was realized with the formation of purified protein crystals. Although crystallization of this mutant was attained other mutant strains were found to be less receptive of the techniques used during the early stages of isolation. Crystal size was found to be diminutive and recrystallization for the sample will need to be performed to increase crystal dimensions for crystallography to be performed. Further development and honing of the procedures for cell cultures, protein isolation and purification was carried out through acclimatizing prior procedures to attain improved realizations of product though each stage of product collection.