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User:Franz St. John
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 an 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
- Stjohn FJ, Rice JD, and Preston JF. (2006). Paenibacillus sp. strain JDR-2 and XynA1: a novel system for methylglucuronoxylan utilization. Appl Environ Microbiol. 2006;72(2):1496-506. DOI:10.1128/AEM.72.2.1496-1506.2006 |
- St John FJ, González JM, and Pozharski E. (2010). Consolidation of glycosyl hydrolase family 30: a dual domain 4/7 hydrolase family consisting of two structurally distinct groups. FEBS Lett. 2010;584(21):4435-41. DOI:10.1016/j.febslet.2010.09.051 |
- St John FJ, Rice JD, and Preston JF. (2006). Characterization of XynC from Bacillus subtilis subsp. subtilis strain 168 and analysis of its role in depolymerization of glucuronoxylan. J Bacteriol. 2006;188(24):8617-26. DOI:10.1128/JB.01283-06 |
- St John FJ, Godwin DK, Preston JF, Pozharski E, and Hurlbert JC. (2009). Crystallization and crystallographic analysis of Bacillus subtilis xylanase C. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009;65(Pt 5):499-503. DOI:10.1107/S1744309109013098 |