Inge Van Molle

Summary

Affiliation: Vrije Universiteit Brussel
Country: Belgium

Publications

  1. pmc Crystallization of the FaeE chaperone of Escherichia coli F4 fimbriae
    Inge Van Molle
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium
    Acta Crystallogr Sect F Struct Biol Cryst Commun 61:427-31. 2005
  2. doi request reprint The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces
    Inge Van Molle
    Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, Brussels, Belgium
    Acta Crystallogr D Biol Crystallogr 65:411-20. 2009
  3. ncbi request reprint The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct
    Joris Messens
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie VIB, Vrije Universiteit Brussel, Pleinlaan 2, B 1050 Brussel, Belgium
    Acta Crystallogr D Biol Crystallogr 60:1180-4. 2004
  4. ncbi request reprint Chloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimers
    Inge Van Molle
    Department of Molecular and Cellular Interactions, Flanders Institute for Biotechnology VIB, Brussels, Belgium
    J Mol Biol 368:791-9. 2007
  5. doi request reprint Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG
    Inge Van Molle
    Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium
    J Mol Biol 394:957-67. 2009
  6. ncbi request reprint Impact of natural variation in bacterial F17G adhesins on crystallization behaviour
    Lieven Buts
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie and Vrije Universiteit Brussel, Pleinlaan 2, B 1050 Brussel, Belgium
    Acta Crystallogr D Biol Crystallogr 61:1149-59. 2005
  7. pmc N-terminal truncation enables crystallization of the receptor-binding domain of the FedF bacterial adhesin
    Maia De Kerpel
    Department of Ultrastructure, Vrije Universiteit Brussel, Flanders Interuniversity Institute for Biotechnology, Pleinlaan 2, 1050 Brussels, Belgium
    Acta Crystallogr Sect F Struct Biol Cryst Commun 62:1278-82. 2006
  8. ncbi request reprint Chaperoning Anfinsen: the steric foldases
    Kris Pauwels
    Department of Molecular and Cellular Interactions, VIB and Department of Ultrastructure, Free University Brussels, Brussels, Belgium
    Mol Microbiol 64:917-22. 2007
  9. ncbi request reprint How thioredoxin can reduce a buried disulphide bond
    Joris Messens
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie VIB, Vrije Universiteit Brussel, Pleinlaan 2, B 1050 Brussels, Belgium
    J Mol Biol 339:527-37. 2004

Detail Information

Publications9

  1. pmc Crystallization of the FaeE chaperone of Escherichia coli F4 fimbriae
    Inge Van Molle
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium
    Acta Crystallogr Sect F Struct Biol Cryst Commun 61:427-31. 2005
    ..4, b = 75.7, c = 69.4 A, beta = 92.8 degrees. Crystals of form 3 were formed in a solution containing the FaeE-FaeG complex and diffract to 2.8 A. Unit-cell parameters are a = 109.7, b = 78.6, c = 87.8 A, beta = 96.4 degrees...
  2. doi request reprint The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces
    Inge Van Molle
    Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, Brussels, Belgium
    Acta Crystallogr D Biol Crystallogr 65:411-20. 2009
    ....
  3. ncbi request reprint The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct
    Joris Messens
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie VIB, Vrije Universiteit Brussel, Pleinlaan 2, B 1050 Brussel, Belgium
    Acta Crystallogr D Biol Crystallogr 60:1180-4. 2004
    ..In order to form a mixed disulfide between ArsC and thioredoxin, a change in the orientation of the TNB-Cys89 disulfide in the structure is necessary...
  4. ncbi request reprint Chloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimers
    Inge Van Molle
    Department of Molecular and Cellular Interactions, Flanders Institute for Biotechnology VIB, Brussels, Belgium
    J Mol Biol 368:791-9. 2007
    ..Furthermore, the structures reveal how FaeG combines the structural requirements of a major fimbrial subunit with its adhesive role by grafting an additional domain on its Ig-like core...
  5. doi request reprint Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG
    Inge Van Molle
    Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium
    J Mol Biol 394:957-67. 2009
    ....
  6. ncbi request reprint Impact of natural variation in bacterial F17G adhesins on crystallization behaviour
    Lieven Buts
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie and Vrije Universiteit Brussel, Pleinlaan 2, B 1050 Brussel, Belgium
    Acta Crystallogr D Biol Crystallogr 61:1149-59. 2005
    ....
  7. pmc N-terminal truncation enables crystallization of the receptor-binding domain of the FedF bacterial adhesin
    Maia De Kerpel
    Department of Ultrastructure, Vrije Universiteit Brussel, Flanders Interuniversity Institute for Biotechnology, Pleinlaan 2, 1050 Brussels, Belgium
    Acta Crystallogr Sect F Struct Biol Cryst Commun 62:1278-82. 2006
    ..20, b = 74.64, c = 99.03 A that diffracted to beyond 2 A resolution. The binding specificity of FedF was screened for on a glycan array, exposing 264 glycoconjugates, to identify specific receptors for cocrystallization with FedF...
  8. ncbi request reprint Chaperoning Anfinsen: the steric foldases
    Kris Pauwels
    Department of Molecular and Cellular Interactions, VIB and Department of Ultrastructure, Free University Brussels, Brussels, Belgium
    Mol Microbiol 64:917-22. 2007
    ..The case of the pilin chaperone is somewhat deviant in that steric information is definitely provided, but the pilus subunit adopts a thermodynamically favourable stable conformation...
  9. ncbi request reprint How thioredoxin can reduce a buried disulphide bond
    Joris Messens
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie VIB, Vrije Universiteit Brussel, Pleinlaan 2, B 1050 Brussels, Belgium
    J Mol Biol 339:527-37. 2004
    ....