Grant: Research Tools and Instruments - Category 1 (<$150,000)
Wilfrid Laurier University
$45,872.00
Crystallization Suite for the Structure Determination of Bacterial Cellulose Biosynthetic Proteins
EF 2011-12
Résumé
This grant will purchase a crystallography suite to support the applicant's research program in the structure-function characterization of bacterial cellulose biosynthetic proteins. Our functional studies are closely intertwined with our structural research as these areas complement each other to provide a detailed understanding of how enzyme activity and substrate binding relates to critical structural folds and/or motifs. The requested crystallography suite will advance our structural research by permitting the efficient generation and identification of X-ray diffraction quality crystals suitable for protein structure determination. Modern programmable incubators will allow for precise control over parameters needed for optimal crystal growth. An innovative stereomicroscope equipped with high magnification, a UV-light module and polarized light filters will greatly enhance our ability to unambiguously distinguish protein crystals from other artifacts in the field of view. The requested camera, software and automated features for the microscope enable specific control over image clarity, acquisition and processing which are important for reliable documentation and assessing crystal growth details related to reproducibility. Cryogenic storage dewars and crystal tools will facilitate the proper cryoprotection of protein crystals in order to minimize damage to crystals during transport and analysis while also providing a means for long-term storage. Thus, the requested instruments will provide a proper crystallization platform that enhances our ability to generate X-ray diffraction quality crystals suitable for protein structure determination. These results will provide a detailed understanding of the biosynthesis of bacterial cellulose and will lead to the discovery of important principles relating to polysaccharide synthesis and biofilm development across bacterial species. This crystallization suite will also serve to create a crystallography resource centre at Wilfrid Laurier University, thereby ensuring that trainees in the field of structure-function biochemistry are equipped with advanced skills/techniques that make them highly competitive upon entering Canada's workforce or pursuing higher education.
Programme
Research Tools and Instruments - Category 1 (<$150,000)
Bénéficiaire
Emplacement
Ontario, Canada
Type de bénéficiaire
Academia
Type
Grant
Source
NSERC's Awards Data
Tel que publié
Application id
422177-2012
Name nom
Weadge, Joel
Department département
Biology
Organization id
35
Institution établissement
Wilfrid Laurier University
Province en
Ontario
Province fr
Ontario
Country en
CANADA
Country fr
CANADA
Fiscal year exercice financier
2011
Competition year année de concours
2012
Award amount
45872
Program id
EQPEQ
Program nane en
Research Tools and Instruments - Category 1 (<$150,000)
Program name fr
Outils et instruments de recherche - catégorie 1 (<150 000$)
Group en
Discovery grants programs
Group fr
Programmes de subventions à la découverte
Committee code
1501
Committee name en
Genes, Cells and Molecules
Committee name fr
Gènes, cellules et molécules
Area of application code
1201
Area of application group en
Advancement of knowledge
Area of application group fr
Avancement des connaissances
Area of application en
Life sciences (including biotechnology)
Area of application fr
Sciences de la vie (y compris biotechnologie)
Research subject code
5404
Research subject group en
Biochemistry
Research subject group fr
Biochimie
Research subject en
Enzymes
Research subject fr
Enzymes
Partie
1
Nb partie
1
Application title
Crystallization Suite for the Structure Determination of Bacterial Cellulose Biosynthetic Proteins
Keyword
NSERC
Application summary
This grant will purchase a crystallography suite to support the applicant's research program in the structure-function characterization of bacterial cellulose biosynthetic proteins. Our functional studies are closely intertwined with our structural research as these areas complement each other to provide a detailed understanding of how enzyme activity and substrate binding relates to critical structural folds and/or motifs. The requested crystallography suite will advance our structural research by permitting the efficient generation and identification of X-ray diffraction quality crystals suitable for protein structure determination. Modern programmable incubators will allow for precise control over parameters needed for optimal crystal growth. An innovative stereomicroscope equipped with high magnification, a UV-light module and polarized light filters will greatly enhance our ability to unambiguously distinguish protein crystals from other artifacts in the field of view. The requested camera, software and automated features for the microscope enable specific control over image clarity, acquisition and processing which are important for reliable documentation and assessing crystal growth details related to reproducibility. Cryogenic storage dewars and crystal tools will facilitate the proper cryoprotection of protein crystals in order to minimize damage to crystals during transport and analysis while also providing a means for long-term storage. Thus, the requested instruments will provide a proper crystallization platform that enhances our ability to generate X-ray diffraction quality crystals suitable for protein structure determination. These results will provide a detailed understanding of the biosynthesis of bacterial cellulose and will lead to the discovery of important principles relating to polysaccharide synthesis and biofilm development across bacterial species. This crystallization suite will also serve to create a crystallography resource centre at Wilfrid Laurier University, thereby ensuring that trainees in the field of structure-function biochemistry are equipped with advanced skills/techniques that make them highly competitive upon entering Canada's workforce or pursuing higher education.