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User:Roland Ludwig

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Roland Ludwig graduated from BOKU - University of Natural Resources and Life Sciences, Vienna with a masters degree in biotechnology and completed his doctoral studies under the supervision of Dietmar Haltrich in 2004. He worked as a senior & key researcher for the Austrian Centre of Industrial Biotechnology until 2009, when starting a postdoctoral internship at Lund University with bioelectrochemist Lo Gorton. Since 2011, he is permanently associated with BOKU and works on cofactor-dependent oxidoreductases such as laccases AA7and GMC-oxidoreductases .

The work focused on structural studies of glycoside hydrolases from families , GH11 and GH12. In 1999 she obtained a personal EMBO fellowship to join the group of ^^^Bernard Henrissat^^^ at the CNRS laboratory Architecture et Fonction des Macromolecules Biologiques. She is currently permanent research engineer in the group of Yves Bourne at the AFMB laboratory. She has determined the crystal structures of
  • GH7 Fusarium oxysporum endoglucanase [2, 3]
  • GH11 Bacillus pumilus xylanase
  • GH12 Streptomyces lividans endoglucanase [4, 5]
  • GH29 Thermotoga maritima α-fucosidase [6]
  • GH109 Elizabethkingia meningosepticum α-N-acetylgalactosaminidase [7]



  1. Gilbert HJ, Stålbrand H, and Brumer H. (2008). How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation. Curr Opin Plant Biol. 2008;11(3):338-48. DOI:10.1016/j.pbi.2008.03.004 | PubMed ID:18430603 [Gilbert2008]
  2. Sulzenbacher G, Driguez H, Henrissat B, Schülein M, and Davies GJ. (1996). Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group. Biochemistry. 1996;35(48):15280-7. DOI:10.1021/bi961946h | PubMed ID:8952478 [Sulzenbacher1996]

All Medline abstracts: PubMed