A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone.

Holdbrook DA, Burmann BM, Huber RG, Petoukhov MV, Svergun DI, Hiller S, Bond PJ
Structure 25(7):1079-1088.e3 (2017 Jul 5)
PMID: 28648612
doi: 10.1016/j.str.2017.05.018 		Submitted to SASBDB: 2016 Jul 24
Published in SASBDB:

SASDB45 – Trimeric periplasmic holdase chaperone protein Skp

Periplasmic holdase chaperone protein Skp experimental SAS data
Trimeric periplasmic holdase chaperone protein Skp Rg histogram
Sample: Periplasmic holdase chaperone protein Skp trimer, 47 kDa Escherichia coli protein
Buffer: 25 mM HEPES 150 mM NaCl 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 24
RgGuinier 3.6 nm
Dmax 12.8 nm
VolumePorod 168 nm3