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Difference between revisions of "User:Gerlind Sulzenbacher"
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Gerlind Sulzenbacher obtained her B.Sc. in Pharmacy from the University of Bologna and completed her PhD under the supervision of Keith Wilson at the University of York, where she worked with [http://www.cazypedia.org/index.php/User:Gideon_Davies/ Gideon Davies], and at the EMBL Hamburg Outstation. The work focused on structural studies of glycoside hydrolases from families [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_7/ GH7], [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_11/ GH11] and [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_12/ GH12]. In 1999 she obtained a personal EMBO fellowship to join the group of [http://www.cazypedia.org/index.php/User:Bernard_Henrissat/ Bernard Henrissat] at the [http://www.cnrs.fr/ CNRS] laboratory [http://www.afmb.univ-mrs.fr/ Architecture et Fonction des Macromolecules Biologiques]. She is currently permanent research engineer in the group of Yves Bourne at the [http://www.afmb.univ-mrs.fr/ AFMB] laboratory. She has determined the crystal structures of | Gerlind Sulzenbacher obtained her B.Sc. in Pharmacy from the University of Bologna and completed her PhD under the supervision of Keith Wilson at the University of York, where she worked with [http://www.cazypedia.org/index.php/User:Gideon_Davies/ Gideon Davies], and at the EMBL Hamburg Outstation. The work focused on structural studies of glycoside hydrolases from families [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_7/ GH7], [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_11/ GH11] and [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_12/ GH12]. In 1999 she obtained a personal EMBO fellowship to join the group of [http://www.cazypedia.org/index.php/User:Bernard_Henrissat/ Bernard Henrissat] at the [http://www.cnrs.fr/ CNRS] laboratory [http://www.afmb.univ-mrs.fr/ Architecture et Fonction des Macromolecules Biologiques]. She is currently permanent research engineer in the group of Yves Bourne at the [http://www.afmb.univ-mrs.fr/ AFMB] laboratory. She has determined the crystal structures of | ||
| − | * [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_7/ GH7] ''Fusarium oxysporum'' endoglucanase <cite>REF1 | + | * [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_7/ GH7] ''Fusarium oxysporum'' endoglucanase <cite>REF1,REF2</cite> |
* [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_11/ GH11] xylanase | * [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_11/ GH11] xylanase | ||
* [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_12/ GH12] endoglucanase | * [http://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_12/ GH12] endoglucanase | ||
Revision as of 07:06, 28 October 2009
Gerlind Sulzenbacher obtained her B.Sc. in Pharmacy from the University of Bologna and completed her PhD under the supervision of Keith Wilson at the University of York, where she worked with Gideon Davies, and at the EMBL Hamburg Outstation. The work focused on structural studies of glycoside hydrolases from families GH7, 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 [1, 2]
- GH11 xylanase
- GH12 endoglucanase
- GH29 α-fucosidase
- GH109 α-N-acetylgalactosaminidase
Reference list
- 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 |
- Sulzenbacher G, Schülein M, and Davies GJ. (1997). Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution. Biochemistry. 1997;36(19):5902-11. DOI:10.1021/bi962963+ |