Crystals of acetylated SecB diffract to 2.3-A 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-A 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.
Dekker
C
C
Department of Biochemistry of Membranes, Department of Crystal and Structural Chemistry, Institute of Biomembranes, Bijvoet Center for Biomolecular Research, Padualaan 8, Utrecht, NL-3584 CH, The Netherlands.
de Kruijff
B
B
de Korte-Kool
G
G
Kroon
J
J
Gros
P
P
D000107:Acetylation; D001426:Bacterial Proteins / Q000737:chemistry*; D003461:Crystallography; D004229:Dithiothreitol / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry; D013058:Mass Spectrometry; D018832:Molecular Chaperones / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D018832:Molecular Chaperones; C057842:SecB protein, Bacteria; D004229:Dithiothreitol