Biological Crystallography Structure of Acostatin, a Dimeric Disintegrin from Southern Copperhead (agkistrodon Contortrix Contortrix), at 1.7 a ˚ Resolution

By N. Moiseeva, R. Bau, S. Swenson, M. Jr., Jun-Yong Choe, Zhi-Jie Liu, M. Allaire

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1. Pavel V. Afonine
2. Paul D. Adams
3. D. Liebschner
4. T. C. Terwilliger
5. Nigel W. Moriarty
6. G. Bunkoczi
7. T. Croll
8. Randy J. Read

Citations in the corpus

• Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix (2019, background): “At ultrahigh resolution (better than 0.7 Å), the interatomic scatterer model can account for residual density from bonding effects (Afonine et al., 2007).”
• Towards automated crystallographic structure refinement with phenix.refine (2012, methodology): “…range of experimental data resolutions from ultrahigh resolution, where an interatomic scatterer (IAS) model can be used to model bonding features (Afonine et al., 2004, 2007), to low resolution, where the use of torsion-angle parameterization (Rice & Brünger, 1994; Grosse-Kunstleve et al.,…”