Figure 1
A plot of the number of native SAD structures deposited per year in the Protein Data Bank. The number shown include both de novo structures and previously solved structures that have been redetermined as part of software and methods development. Excluded from the list are standard proteins such as insulin, lysozyme, thaumatin, trypsin and glucose isomerase. The peak in native SAD structure determinations during the period from 2004 to 2009 reflects, among other things, the introduction of the Rigaku chromium-rotating anode, which was used by the SECSG (Adams et al., 2003) and SGC (Yakunin et al., 2004) structural genomics centers, and the work carried out by Cheng Yang at Rigaku and Nobuhisa Watanabe at Hokkaido University, Japan. The large spike in PDB entries in 2006 reflects ten structures reported in a methods-development paper (Mueller-Dieckmann et al., 2007), which first noted that chloride, sulfate, phosphate or metal ions present in the crystal can contribute to the anomalous signal in the data. The large increase in PDB depositions for 2014 reflects the proteins used for the development of multi-data-set averaging (from single or multiple crystals) methods, with 11 structures representing the SLS studies reported in 2014 (Weinert et al., 2015). |