@article{37747a0070784f33aea79120353038db,
title = "The periplasmic E. coli chaperone Skp is a trimer in solution: Biophysical and preliminary crystallographic characterization",
abstract = "The 'seventeen kilodalton protein' Skp confers transient solubility on outer membrane proteins during biogenesis in Gram-negative bacteria. Here we report a first biophysical characterization of this chaperone itself, which also possesses biotechnological potential in the production of recombinant proteins. Using cross-linking and gel filtration methods, we found that Skp forms a stable homo-trimer in solution. Following thermal denaturation, monitored by CD spectroscopy, this chaperone refolds with high efficiency but exhibits a pronounced hysteresis between the un- and refolding transitions. Using the recombinant protein equipped with the Strep-tag II at its N-terminus, suitable crystallization conditions for Skp were found. A first data set was collected to 2.60 {\AA} resolution.",
keywords = "Circular dichroism, Cross-linking, Outer membrane protein, Protein folding, Strep-tag, Thermal denaturation",
author = "Martin Schlapschy and Dommel, {Monica K.} and Kamyar Hadian and Marton Fogarasi and Kornd{\"o}rfer, {Ingo P.} and Arne Skerra",
note = "Funding Information: The authors wish to thank I. Theobald for preparation of strept-avidin affinity columns and the staff at BW7A at DESY (Hamburg, Germany) for technical aid. This work was supported by the {\textquoteleft}European Community – Access to Research Infrastructure Action of the Improving Human Potential Programme to the EMBL Hamburg Outstation, contract number HPRI-CT-1999-00017{\textquoteright} and by the {\textquoteleft}Fonds der Chemischen Industrie{\textquoteright}.",
year = "2004",
month = feb,
doi = "10.1515/BC.2004.032",
language = "English",
volume = "385",
pages = "137--143",
journal = "Biological Chemistry",
issn = "1431-6730",
publisher = "Walter de Gruyter GmbH",
number = "2",
}