Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome.

Silva NSM, Seraphim TV, Minari K, Barbosa LRS, Borges JC
Int J Biol Macromol 108:193-204 (2018 Mar)
PMID: 29191421
doi: 10.1016/j.ijbiomac.2017.11.161 		Submitted to SASBDB: 2017 Jun 17
Published in SASBDB:

SASDC55 – Plasmodium falciparum p23A

CS domain protein, putative experimental SAS data
DAMFILT model
Sample: CS domain protein, putative monomer, 19 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 2 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.4
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 May 26
RgGuinier 2.5 nm
Dmax 8.5 nm

SASDC65 – Plasmodium falciparum p23B

Co-chaperone p23 experimental SAS data
DAMFILT model
Sample: Co-chaperone p23 monomer, 31 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 2 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.4
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 May 26
RgGuinier 3.7 nm
Dmax 13.0 nm