| MWexperimental | 15 | kDa |
| MWexpected | 13 | kDa |
| VPorod | 23 | nm3 |
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log I(s)
2.51×104
2.51×103
2.51×102
2.51×101
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s, nm-1
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M. tuberculosis class II apurinic/ apyrimidinic-endonuclease/3'-5' exonuclease (XthA) engages with NAD+-dependent DNA ligase A (LigA) to counter futile cleavage and ligation cycles in base excision repair.
Khanam T, Afsar M, Shukla A, Alam F, Kumar S, Soyar H, Dolma K, Pasupuleti M, Srivastava KK, Ampapathi RS, Ramachandran R, Nucleic Acids Res (2020) Europe PMCSASDD88 – The BRCT domain from Mycobacterium tuberculosis DNA ligase
M.tb. LigA BRCT domain (DNA ligase A)|
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Fits and models
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In house laboratory SAXS data from a solution of the BRCT domain from M. tuberculosis DNA ligase in 50 mM Tris-HCl 500 mM NaCl 5mM β-mercaptoethanol, pH 8 were collected using an Anton Paar SAXSpace instrument at the CSIR-Central Drug Research Institute (Lucknow, India) using a Dectris Mythen 2R1K detector at a sample-detector distance of 0.3 m and at a wavelength of λ = 0.154 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 10.00 mg/ml was measured at 10°C. Two successive 1800 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
The experimental molecular weight quoted for this entry was evaluated using calibrated size-exclusion chromatography (GE Healthcare Superdex75 10/30 column). The atomistic models displayed in this entry (ribbon format) are a parent Phyre2 protein homology model (top) and one of ten structures obtained from the parent after elNémo normal mode calculations (bottom). Refer to: Kelley et al. (2015) Nature Protocols 10, 845-858; Suhre & Sanejouand (2004) Nucleic Acids Res. 32(Web Server issue): W610–W614. |
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