Crystallization and Preliminary X-ray Crystallographic Studies of the Oligomeric Death-Domain Complex Between PIDD and RAIDD
Journal Article
·
· Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Three large macromolecular complexes known as the death-inducing signaling complex (DISC), the apoptosome and the PIDDosome mediate caspase activation in apoptosis signaling pathways. The PIDDosome, which activates caspase-2, is composed of three protein components: PIDD, RAIDD and caspase-2. Within the PIDDosome, the interaction between PIDD and RAIDD is mediated by a homotypic interaction between their death domains (DDs). PIDD DD and RAIDD DD were overexpressed in Escherichia coli with engineered C-terminal His tags. The proteins were purified and mixed to allow complex formation. Gel-filtration and multi-angle light scattering (MALS) analyses showed that the complex is around 150 kDa in solution. The purified PIDD DD-RAIDD DD complex was crystallized at 293 K. X-ray diffraction data were collected to resolutions of 3.2 and 4.0 {angstrom} from a native and a Hg-derivative crystal, respectively. The crystals belong to space group P6{sub 5}, with unit-cell parameters a = b = 138.4, c = 207.6 {angstrom}.
- Research Organization:
- Brookhaven National Laboratory (BNL) National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 929889
- Report Number(s):
- BNL--80471-2008-JA
- Journal Information:
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Journal Name: Acta Crystallographica Section F: Structural Biology and Crystallization Communications Vol. 63
- Country of Publication:
- United States
- Language:
- English
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