Crystals of Acetylated SecB Diffract to 2.3-Å Resolution

The molecular chaperone SecB is part of the protein translocation pathway in Escherichia coli. SecB was purified from an overproducing strain and crystallized, resulting in crystals diffracting to 2.3-Å resolution. The analysis of electrospray ionization mass spectra of dissolved crystals of SecB in...

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Bibliographic Details
Published in:Journal of structural biology 1999-12, Vol.128 (3), p.237-242
Main Authors: Dekker, Carien, de Kruijff, Ben, de Korte-Kool, Gerda, Kroon, Jan, Gros, Piet
Format: Article
Language:English
Subjects:
Acetylation
Bacterial Proteins - chemistry
chaperone
crystallization
Crystallography
Dithiothreitol - metabolism
electrospray ionization mass spectrometry
Escherichia coli - chemistry
Mass Spectrometry
Molecular Chaperones - chemistry
Protein Conformation
Protein Folding
SecB
X-Ray Diffraction
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Summary:The molecular chaperone SecB is part of the protein translocation pathway in Escherichia coli. SecB was purified from an overproducing strain and crystallized, resulting in crystals diffracting to 2.3-Å resolution. The analysis of electrospray ionization mass spectra of dissolved crystals of SecB indicated that we have crystallized an acetylated form of SecB. Sequence analysis suggests that the protein is fully acetylated at its N-terminus in vivo, indicating that potential deacetylation is artificially introduced by purification methods. The high degree of acetylation that we observed might account for the fact that the crystals obtained as described in this study diffract to higher resolution than those in previously reported trials.
ISSN:1047-8477
1095-8657
DOI:10.1006/jsbi.1999.4179