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Difference between revisions of "User:Franz St. John"
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| − | Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This research focused primarily on the microbiological characterisation of novel xylan-utilising Gram-positive bacteria. Following as interest in protein structure and function studies he accepted a post-doctoral research fellowship position under the guidance of Dr. Edwin Pozharski at the x-ray crystallography core facility in the Department of Pharmaceutical Sciences of the University of Maryland, Baltimore. In this position Franz was able to study the structures of xylanases from two different glycosyl hydrolase families. In 2009 Franz took a permanent research microbiologist position at the Forest Products Laboratory in Madison, WI. In this position, his research will focus on the identification of novel enzymes involved in the degradation of lignocellulosic biomass and their complete functional characterisation and potential application in lignocellulose bioconversion processes. Franz has recently published a work to revise the classification of GH30 and GH5 enzymes and has determined the crystal structures of | + | Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This research focused primarily on the microbiological characterisation of novel xylan-utilising Gram-positive bacteria. Following as interest in protein structure and function studies he accepted a post-doctoral research fellowship position under the guidance of Dr. Edwin Pozharski at the x-ray crystallography core facility in the Department of Pharmaceutical Sciences of the University of Maryland, Baltimore. In this position Franz was able to study the structures of xylanases from two different glycosyl hydrolase families. In 2009 Franz took a permanent research microbiologist position at the Forest Products Laboratory in Madison, WI. In this position, his research will focus on the identification of novel enzymes involved in the degradation of lignocellulosic biomass and their complete functional characterisation and potential application in lignocellulose bioconversion processes. Franz has recently published a work to revise the classification of [[GH30]] and [[GH5]] enzymes and has determined the crystal structures of |
| − | * XynC, a GH30 glucuronoxylan xylanohydrolase (previously of GH5) of ''Bacillus subtilis'' 168 | + | * XynC, a GH30 glucuronoxylan xylanohydrolase (previously of [[GH5]]) of ''Bacillus subtilis'' 168 |
| − | * XynA<sub>1</sub>CD, the GH10 catalytic module from xylanase A1 of ''Paenibacillus'' sp. JDR-2 | + | * XynA<sub>1</sub>CD, the [[GH10]] catalytic module from xylanase A1 of ''Paenibacillus'' sp. JDR-2 |
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| + | [[Category:Contributors|St.John,Franz]] | ||
Revision as of 13:37, 19 October 2010
Franz St John received a PhD in Microbiology from the Department of Microbiology and Cell Science at the University of Florida in the laboratory of Dr. James F. Preston. This research focused primarily on the microbiological characterisation of novel xylan-utilising Gram-positive bacteria. Following as interest in protein structure and function studies he accepted a post-doctoral research fellowship position under the guidance of Dr. Edwin Pozharski at the x-ray crystallography core facility in the Department of Pharmaceutical Sciences of the University of Maryland, Baltimore. In this position Franz was able to study the structures of xylanases from two different glycosyl hydrolase families. In 2009 Franz took a permanent research microbiologist position at the Forest Products Laboratory in Madison, WI. In this position, his research will focus on the identification of novel enzymes involved in the degradation of lignocellulosic biomass and their complete functional characterisation and potential application in lignocellulose bioconversion processes. Franz has recently published a work to revise the classification of GH30 and GH5 enzymes and has determined the crystal structures of
- XynC, a GH30 glucuronoxylan xylanohydrolase (previously of GH5) of Bacillus subtilis 168
- XynA1CD, the GH10 catalytic module from xylanase A1 of Paenibacillus sp. JDR-2