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Figure 1
XIAP is a compact homodimer in solution. (a) Experimental CD spectrum (black) of full-length XIAP (2.2 µM, 298 K) and BeStSel fitting (red). The secondary-structure content estimated from the fitting is shown. (b) SEC-MALS elution profile of full-length XIAP (30 µM, 298 K). The refractive index is shown in black; the calculated molecular mass of the XIAP dimer peak is shown in red. (c) 1H–15N HSQC NMR spectrum of the full-length XIAP homodimer acquired at a dimer concentration of 80 µM at 700 MHz and 310 K. ∼70 amide cross-peaks are detected in the central region of the spectrum, typical of unstructured proteins. No signals are detected from the folded domains owing to relaxation-induced broadening beyond detection.

IUCrJ
Volume 6| Part 5| September 2019| Pages 948-957
ISSN: 2052-2525
https://doi.org/10.1107/S205225251901073X