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, UCB or SCRI. Protein from successful targets will be sent to UCB 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 WSU and UW-PPG. Large protein-protein complexes will be solved by Cryo-electron microscopy at UW-CryoEM.
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. All protocols are available for view. 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).
Really excited that our article describing the structure, function and antigenicity of the SARS-CoV-2 spike glycopr… https://t.co/AAUAeN0INw
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