New material in the second online edition of Volume F

There are 19 new chapters in this second edition of Volume F:

• 2.2. Quality indicators in macromolecular crystallography: definitions and applications (H. M. Einspahr and M. S. Weiss)
• 3.2. Expression and purification of membrane proteins for structural studies (J. A. Ernst, D. G. Yansura and C. M. Koth)
• 4.3. Application of protein engineering to enhance crystallizability and improve crystal properties (Z. S. Derewenda)
• 4.4. High-throughput X-ray crystallography (K. H. Choi)
• 9.2. Robotic crystal loading (T. Earnest and C. Cork)
• 9.3. X-ray diffraction imaging of whole cells (D. Shapiro)
• 10.3. Radiation damage (E. F. Garman)
• 11.7. Detecting twinning by merohedry (T. O. Yeates and Y. Tsai)
• 13.5. Molecular replacement with MOLREP (A. Vagin and A. Teplyakov)
• 16.3. Ab initio phasing of low-resolution Fourier syntheses (V. Y. Lunin, A. G. Urzhumtsev and A. Podjarny)
• 17.1. Macromolecular model building and validation using Coot (P. Emsley, B. Lohkamp and K. Cowtan)
• 18.10. PrimeX and the Schrödinger computational chemistry suite of programs (J. A. Bell, Y. Cao, J. R. Gunn, T. Day, E. Gallicchio, Z. Zhou, R. Levy and R. Farid)
• 18.11 PHENIX: a comprehensive Python-based system for macromolecular structure solution (P. D. Adams, P. V. Afonine, G. Bunkóczi, V. B. Chen, I. W. Davis, N. Echols, J. J. Headd, L.-W. Hung, G. J. Kapral, R. W. Grosse-Kunstleve, A. J. McCoy, N. W. Moriarty, R. Oeffner, R. J. Read, D. C. Richardson, J. S. Richardson, T. C. Terwilliger and P. H. Zwart)
• 18.12. Structure determination in the presence of twinning by merohedry (T. O. Yeates and M. R. Sawaya)
• 19.8. Use of SPIDER and SPIRE in image reconstruction (A. Leith, W. Baxter and J. Frank)
• 19.9. Four-dimensional cryo-electron microscopy at quasi-atomic resolution: IMAGIC 4D (M. van Heel, R. Portugal, A. Rohou, C. Linnemayr, C. Bebeacua, R. Schmidt, T. Grant and M. Schatz)
• 19.10. Single-particle reconstruction with EMAN (S. Ludtke)
• 21.6. MolProbity: all-atom structure validation for macromolecular crystallography (V. B. Chen, W. B. Arendall III, J. J. Headd, D. A. Keedy, R. M. Immormino, G. J. Kapral, L. W. Murray, J. S. Richardson and D. C. Richardson )
• 23.6. Halogen interactions in biomolecular crystal structures (M. J. Vallejos, P. Auffinger and P. S. Ho)

In addition, the following chapters have been revised:

• 1.1. Overview (E. Arnold, D. M. Himmel and M. G. Rossmann)
• 1.4. Perspectives for the future (E. Arnold, M. G. Rossmann, D. M. Himmel, J. C. H. Spence and S. Sun)
• 4.1. General methods of crystallization (C. Sauter, B. Lorber, A. McPherson and R. Giegé)
• 8.1. Synchrotron-radiation instrumentation, methods and scientific utilization (J. R. Helliwell)
• 9.1. Principles of monochromatic data collection (Z. Dauter and K. S. Wilson)
• 10.1. Introduction to cryocrystallography (H. Hope and S. Parkin)
• 11.3. Integration, scaling, space-group assignment and post refinement (W. Kabsch)
• 11.4. DENZO and SCALEPACK (Z. Otwinowski, W. Minor, D. Borek and M. Cymborowski)
• 11.6. XDS (W. Kabsch)
• 13.3. Translation functions (L. Tong)
• 15.1. Phase improvement by iterative density modification (K. Y. J. Zhang, K. D. Cowtan and P. Main)
• 15.2. Model phases: probabilities, bias and maps (R. J. Read)
• 16.1. Ab initio phasing (G. M. Sheldrick, C. J. Gilmore, H. A. Hauptman, C. M. Weeks, R. Miller and I. Usón)
• 18.4. Refinement at atomic resolution (Z. Dauter, G. N. Murshudov and K. S. Wilson)
• 18.7. The TNT refinement package (D. E. Tronrud and L. F. Ten Eyck)
• 18.8. ARP/wARP - automated model building and refinement (V. S. Lamzin, A. Perrakis and K. S. Wilson)
• 18.9. Macromolecular applications of SHELX (G. M. Sheldrick)
• 19.5. Fibre diffraction (R. Chandrasekaran and G. Stubbs)
• 19.6. Electron cryomicroscopy of biological macromolecules (T. S. Baker and R. Henderson)
• 21.5. KiNG and kinemages (V. B. Chen, J. S. Richardson and D. C. Richardson)
• 22.3. Hydrogen bonding in biological macromolecules (E. N. Baker)
• 23.1. Protein-fold classification (C. Orengo and J. Thornton)
• 23.5. Solvent structure (C. Mattos and D. Ringe)
• 24.1. The Worldwide Protein Data Bank (H. M. Berman, K. Henrick, G. Kleywegt, H. Nakamura and J. Markley)
• 24.2. The Nucleic Acid Database (B. Schneider, J. de la Cruz, S. Dutta, Z. Feng, L. Chen, J. Westbrook, H. Yang, J. Young, C. Zardecki and H. M. Berman)
• 24.3. The Biological Macromolecule Crystallization Database (D. T. Gallagher and M. Tung)

All known errors in the first edition have also been corrected.