Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering.

Seraphim TV, Silva KP, Dores-Silva PR, Barbosa LR, Borges JC
Int J Biol Macromol 97:503-512 (2017 Apr)

PMID: 28104372 doi: 10.1016/j.ijbiomac.2017.01.058

Submitted to SASBDB: 2016 Jan 18 Published in SASBDB: 2016 Jan 21

SASDBD3 – Leishmania braziliensis heat shock protein 90 (Hsp90). Sample: Leishmania braziliensis heat shock protein 90 (Hsp90) dimer, 166 kDa Leishmania braziliensis protein Buffer: 25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5 Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1 RgGuinier 5.3 nm Dmax 21.0 nm VolumePorod 380 nm3

SASDBE3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N domain. Sample: Leishmania braziliensis heat shock protein 90 (Hsp90) N domain monomer, 26 kDa Leishmania braziliensis protein Buffer: 25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5 Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1 RgGuinier 2.0 nm Dmax 7.5 nm VolumePorod 40 nm3

SASDBF3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains. Sample: Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains monomer, 62 kDa Leishmania braziliensis protein Buffer: 25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5 Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1 RgGuinier 3.2 nm Dmax 13.0 nm VolumePorod 89 nm3