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-Structure paper
Title | Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems |
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Journal, issue, pages | Year 2018 Jan 25 |
Publish date | Mar 17, 2014 (data collection date) |
Authors | Tuukkanen A / Freire D / Chan S / Arbing M / Reed R / Evans T / Zenkeviciutė G / Kim J / Kahng S / Sawaya M ...Tuukkanen A / Freire D / Chan S / Arbing M / Reed R / Evans T / Zenkeviciutė G / Kim J / Kahng S / Sawaya M / Wilmanns M / Eisenberg D / Parret A |
External links | Publisher's page / Search PubMed |
Methods | SAS (X-ray synchrotron) |
Structure data | SASDDQ2: EspG3 chaperone from Mycobacterium marinum (EspG3 chaperone from Mycobacterium marinum M, EspG3Mm) SASDDR2: EspG1 chaperone from Mycobacterium marinum (EspG1 from Mycobacterium marinum, EspG1Mm) SASDDS2: EspG3 chaperone from Mycobacter smegmatis (EspG3 chaperone from Mycobacterium smegmatis, EspG3Msm) SASDDT2: EspG3 chaperone from Mycobacterium tuberculosis (EspG3Mtb) SASDDU2: EspG3 chaperone from Mycobacterium smegmatis (Sel-Met labelled) SASDDV2: EspG5 chaperone from Mycobacterium tuberculosis (EspG5Mtb) SASDDX2: EspG3-PE5/PPE4 complex from M. tuberculosis (EspG3 chaperone from Mycobacterium tuberculosis, EspG3Mtb + PE5 from Mycobacterium tuberculosis, PE5 + PPE4 from Mycobacterium tuberculosis, PPE4) |
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