CRYSTAL COLLECTION OF BAK AND CCBL UBA DOMAIN

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Bcl-2 homologous antagonist killer (Bak) is a pro-apoptotic member of the B cell lymphoma (Bcl) family of proteins which is directly implicated in many pathologies related to aberant apoptosis (e.g. cancer and neurodegeneration). Any structural information related to Bak is crucial for the understanding of its functional role and we have obtained a previous structure and would like to follow up with a derivatized Bak crystal that diffracts on our home source at best at 3A. We hope to bring the resolution `down` to improve the refinement statistics. cCBL and CBL-b are adaptors for the tyrosine kinase receptors (Met receptors - cancer related), which contain a Ubiquitin E3 ligase domain and a C-terminal UBA domain. Interestingly, c-CBL UBA does not bind ubiquitin whereas the CBL-b UBA does.