TY  - JOUR
A1  - Mietrach, Nicole
A1  - Schlosser, Andreas
A1  - Geibel, Sebastian
T1  - An extracellular domain of the EsaA membrane component of the type VIIb secretion system: expression, purification and crystallization
JF  - Acta Crystallographica Section F
N2  - The membrane protein EsaA is a conserved component of the type VIIb secretion system. Limited proteolysis of purified EsaA from Staphylococcus aureus USA300 identified a stable 48 kDa fragment, which was mapped by fingerprint mass spectrometry to an uncharacterized extracellular segment of EsaA. Analysis by circular dichroism spectroscopy showed that this fragment folds into a single stable domain made of mostly α‐helices with a melting point of 34.5°C. Size‐exclusion chromatography combined with multi‐angle light scattering indicated the formation of a dimer of the purified extracellular domain. Octahedral crystals were grown in 0.2 M ammonium citrate tribasic pH 7.0, 16% PEG 3350 using the hanging‐drop vapor‐diffusion method. Diffraction data were analyzed to 4.0 Å resolution, showing that the crystals belonged to the enantiomorphic tetragonal space groups P41212 or P43212, with unit‐cell parameters a = 197.5, b = 197.5, c = 368.3 Å, α = β = γ = 90°.
KW  - ESAT‐6‐like secretion system
KW  - ESS
KW  - type VII secretion system
KW  - EsaA
KW  - extracellular domain
KW  - Staphylococcus aureus USA300
Y1  - 2019
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-213681
VL  - 75
IS  - 12
ER  -