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Start Over Author "Busso Didier" Journal acta crystallographica section d biological crystallography
5 results on '"Busso Didier"'

1. Co-expression of protein complexes in prokaryotic and eukaryotic hosts: experimental procedures, database tracking and case studies

Author

Romier, Christophe, primary, Ben Jelloul, Marouane, additional, Albeck, Shira, additional, Buchwald, Gretel, additional, Busso, Didier, additional, Celie, Patrick H. N., additional, Christodoulou, Evangelos, additional, De Marco, Valeria, additional, van Gerwen, Suzan, additional, Knipscheer, Puck, additional, Lebbink, Joyce H., additional, Notenboom, Valerie, additional, Poterszman, Arnaud, additional, Rochel, Natacha, additional, Cohen, Serge X., additional, Unger, Tamar, additional, Sussman, Joel L., additional, Moras, Dino, additional, Sixma, Titia K., additional, and Perrakis, Anastassis, additional

Published
2006
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2. Recombinant protein expression and solubility screening in Escherichia coli: a comparative study

Author

Berrow, Nick S., primary, Büssow, K., additional, Coutard, B., additional, Diprose, J., additional, Ekberg, M., additional, Folkers, G. E., additional, Levy, N., additional, Lieu, V., additional, Owens, R. J., additional, Peleg, Y., additional, Pinaglia, C., additional, Quevillon-Cheruel, S., additional, Salim, L., additional, Scheich, C., additional, Vincentelli, R., additional, and Busso, Didier, additional

Published
2006
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5. Structure of OsmC from Escherichia coli: a salt-shock-induced protein.

Author

Shin DH, Choi IG, Busso D, Jancarik J, Yokota H, Kim R, and Kim SH

Subjects
Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Peroxidases chemistry, Peroxidases metabolism, Peroxiredoxins, Protein Conformation, Salts, Sequence Homology, Amino Acid, Structural Homology, Protein, Escherichia coli Proteins chemistry, Escherichia coli Proteins metabolism
Abstract

The crystal structure of an osmotically inducible protein (OsmC) from Escherichia coli has been determined at 2.4 A resolution. OsmC is a representative protein of the OsmC sequence family, which is composed of three sequence subfamilies. The structure of OsmC provides a view of a salt-shock-induced protein. Two identical monomers form a cylindrically shaped dimer in which six helices are located on the inside and two six-stranded beta-sheets wrap around these helices. Structural comparison suggests that the OsmC sequence family has a peroxiredoxin function and has a unique structure compared with other peroxiredoxin families. A detailed analysis of structures and sequence comparisons in the OsmC sequence family revealed that each subfamily has unique motifs. In addition, the molecular function of the OsmC sequence family is discussed based on structural comparisons among the subfamily members.

Published
2004
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