Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.

Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL
Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019 Mar 1)

PMID: 30950400 doi: 10.1107/S2059798319000081

Submitted to SASBDB: 2018 Sep 18 Published in SASBDB: 2019 Mar 29

SASDEK4 – C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein (ScsC) Sample: C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein monomer, 20 kDa Proteus mirabilis protein Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4 Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5 RgGuinier 1.7 nm Dmax 5.4 nm VolumePorod 22200 nm3

SASDER4 – Wild-type suppressor of copper sensitivity C protein, PmScsC, with concentration series data Sample: Suppressor of Copper Sensitivity C protein trimer, 74 kDa Proteus mirabilis protein Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4 Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5 RgGuinier 3.7 nm Dmax 11.1 nm VolumePorod 101 nm3

SASDEQ4 – Deletion mutant of the suppressor of copper sensitivity C protein, PmScsC, with concentration series data Sample: Deletion mutant of PmScsC, 23 kDa Proteus mirabilis protein Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4 Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5 RgGuinier 2.6 nm Dmax 9.0 nm VolumePorod 54 nm3