The target selection team will use a series of bioinformatic and manual filters to select ~500 targets each year for entry into the protein production and structure determination pipeline. Each target will undergo cloning & expression testing and protein production at UW-PPG, Beryllium or CIDResearch using a multi-pronged serial escalation approach. Protein from successful targets will be sent to Beryllium for crystallization screening and pre-qualified crystal samples sent to the synchrotron beam-lines data X-ray structure solution. A small number of high priority targets from proteins that fail to crystallize will be selected for NMR analysis at Battelle and UW-PPG.
We anticipate that these approaches will yield 75-90 protein structures per year, including several structures of the same protein(s) with different ligands. All structures will be submitted to the Protein Data Bank (PDB), and all materials (clones and protein) generated will be publicly available. Experimental procedures and weekly target status reports will be submitted to the TargetTrack database. View all protocols.Metrics for deposition of X-ray crystal structures into the PDB are agreed upon between the two NIAID-funded structural genomics for infectious disease centers (SSGCID and the CSGID).
From our own Jan Abendroth, a user-friendly test case in which an unknown protein fragment could be determined usin… https://t.co/pIZmebDiEi
1 week, 5 days ago
Nucleoside diphosphate kinase from Borrelia burgdorferi prepared in a transition-state complex with ADP and vanadat… https://t.co/ESh4gPtH7f
3 months, 4 weeks ago