Determination of Protein Structures—A Series of Fortunate Events

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Determination of Protein Structures—A Series of Fortunate Events Maksymilian Chruszcz, Alexander Wlodawer, Wladek Minor Biophysical Journal Volume 95, Issue 1, Pages 1-9 (July 2008) DOI: 10.1529/biophysj.108.131789 Copyright © 2008 The Biophysical Society Terms and Conditions

Figure 1 The fraction of x-ray structures deposited in the PDB that report the use of synchrotron sources for their determination (dark blue) and sample temperatures close to 100K during data collection (light blue). Biophysical Journal 2008 95, 1-9DOI: (10.1529/biophysj.108.131789) Copyright © 2008 The Biophysical Society Terms and Conditions

Figure 2 Residue 160 in the crystal structure of soybean lipoxygenase shown together with 2Fo-Fc electron density map. (A) A map contoured at 1σ level. The crystal was obtained using natural protein isolated from soybeans and the residue was identified as serine (PDB codes: 1YGE and 1F8N). (B) Map shown at 0.7σ. The serine was replaced by glutamic acid, what is consistent with results of the DNA sequencing (Ted Holman, 2007, private communication). (C) Electron density shown at 0.3σ. Different contouring of the map reveals either possible decarboxylation during data collection or conformational flexibility of Glu160. Biophysical Journal 2008 95, 1-9DOI: (10.1529/biophysj.108.131789) Copyright © 2008 The Biophysical Society Terms and Conditions

Figure 3 Comparison of the extent of application of SAD and MAD techniques in APS and ESRF, as reported in PDB. Biophysical Journal 2008 95, 1-9DOI: (10.1529/biophysj.108.131789) Copyright © 2008 The Biophysical Society Terms and Conditions