Projecten per jaar
The Escherichia coli rnlAB operon encodes a toxin-antitoxin module that is involved in protection against infection by bacteriophage T4. The full-length RnlA-RnlB toxin-antitoxin complex as well as the toxin RnlA were purified to homogeneity and crystallized. When the affinity tag is placed on RnlA, RnlB is largely lost during purification and the resulting crystals exclusively comprise RnlA. A homogeneous preparation of RnlA-RnlB containing stoichiometric amounts of both proteins could only be obtained using a His tag placed C-terminal to RnlB. Native mass spectrometry and SAXS indicate a 1:1 stoichiometry for this RnlA-RnlB complex. Crystals of the RnlA-RnlB complex belonged to space group C2, with unit-cell parameters a = 243.32, b = 133.58, c = 55.64Å, β = 95.11°, and diffracted to 2.6Å resolution. The presence of both proteins in the crystals was confirmed and the asymmetric unit is likely to contain a heterotetramer with RnlA2:RnlB2 stoichiometry.
|Tijdschrift||Acta Crystallographica Section F - Structural Biology Communications|
|Status||Published - jan 2020|
VingerafdrukDuik in de onderzoeksthema's van 'The Escherichia coli RnlA–RnlB toxin–antitoxin complex: production, characterization and crystallization'. Samen vormen ze een unieke vingerafdruk.
1/01/15 → 31/12/18
Charlier, D., Wilmaerts, D., Michiels, J. & Loris, R., 9 jul 2021, In: Nucleic Acids Research. 49, 12, blz. 7164-7178 15 blz.
Onderzoeksoutput: Article › peer reviewOpen AccessBestand1 Citaat (Scopus)78 Downloads (Pure)
Regulatory mechanisms behind the activities of bacterial HEPN ribonuclease RnlA and ParE2 gyrase poisonGarcia Rodriguez, G., 2020
Onderzoeksoutput: PhD Thesis
- 1 Participation in workshop, seminar