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International Tables for Crystallography (2019). Vol. H. ch. 7.1, pp. 718-736
https://doi.org/10.1107/97809553602060000975 |
Chapter 7.1. Macromolecular powder diffraction
Contents
- 7.1. Macromolecular powder diffraction (pp. 718-736) | html | pdf | chapter contents |
- 7.1.1. Introduction (p. 718) | html | pdf |
- 7.1.2. Sample preparation and handling (pp. 718-720) | html | pdf |
- 7.1.3. Data collection (pp. 720-721) | html | pdf |
- 7.1.4. Cryo-cooling protein powder samples and microstructural effects (pp. 721-723) | html | pdf |
- 7.1.5. Crystal screening (pp. 723-725) | html | pdf |
- 7.1.6. Improvements in data quality via the use of multiple profiles (pp. 725-726) | html | pdf |
- 7.1.7. Structure solution (pp. 726-729) | html | pdf |
- 7.1.8. Structure refinement (pp. 729-731) | html | pdf |
- 7.1.9. Related developments (pp. 731-732) | html | pdf |
- 7.1.10. Concluding remarks (p. 732) | html | pdf |
- References | html | pdf |
- Figures
- Fig. 7.1.1. Optical-microscopy images of needle-shaped crystals of the nonstructural protein 3 (nsP3) macro domain of the Mayaro virus (MAYV) grown under different conditions (Papageorgiou et al (p. 719) | html | pdf |
- Fig. 7.1.2. (a) A bunch of needle-shaped MAYV crystals as grown within single `urchins' (p. 720) | html | pdf |
- Fig. 7.1.3. Low-angle region of powder-diffraction patterns from lysozyme samples (p. 720) | html | pdf |
- Fig. 7.1.4. Projections of the electron density in the ab plane for TEWL at room temperature (left) and low temperature (right) (p. 722) | html | pdf |
- Fig. 7.1.5. Upper left panel: The Rietveld fit for tetragonal HEWL at 100 K with a mixture of PEG 400 and methanol added for cryoprotection [λ = 1.250845 (23) Å, ID31, ESRF, GSAS: space group: P43212, a = 78.31382 (6), c = 36.8870 (7) Å, Rwp = 6.74%, R(F2) = 9.66%] (p. 723) | html | pdf |
- Fig. 7.1.6. Colour representation of ID31 powder-diffraction data from the pH variation experiment, from pH 6.56 to 3.33, of HEWL crystallized at 277 K (a) and room temperature (b) (p. 724) | html | pdf |
- Fig. 7.1.7. The tetrameric form of urate oxidase (Uox) co-crystallized with its inhibitor 8-azaxanthine (PDB code: 1r51 , space group: I222, a = 81.30, b = 96.30, c = 105.60 Å) (Retailleau et al (p. 725) | html | pdf |
- Fig. 7.1.8. A view of the N-acetylglucosamine complex with HEWL as determined from high-resolution X-ray powder-diffraction data (Von Dreele, 2001, 2005) (p. 725) | html | pdf |
- Fig. 7.1.9. A schematic view down the c axis of the doubled-c-axis variant of the T3R3 Zn–insulin complex as determined from powder-diffraction data (Von Dreele et al (p. 727) | html | pdf |
- Fig. 7.1.10. Powder-diffraction structure of the ponsin SH3.2 domain (p. 727) | html | pdf |
- Fig. 7.1.11. The electron-density map of HEWL (green) obtained from MIR data after density modification superimposed onto the known molecular structure (orange) obtained from the PDB (PDB code: 6lyt ; Young et al (p. 728) | html | pdf |
- Fig. 7.1.12. X-ray powder-diffraction profile from the final Rietveld refinement of whale metmyoglobin (p. 729) | html | pdf |
- Fig. 7.1.13. Selected regions of the final refined structural model of the second SH3 domain of ponsin in stick representation and the corresponding total omit map contoured at 1σ (p. 729) | html | pdf |
- Fig. 7.1.14. Upper panel: Powder-diffraction structure of the T6 bovine insulin (BI) hexamer (p. 730) | html | pdf |
- Fig. 7.1.15. Evolution of selected amino acids along the protein chains during the Rietveld refinement procedure for T6 BI in GSAS (p. 731) | html | pdf |
- Tables
- Table 7.1.1. Synchrotron beamlines used for protein powder measurements and their key characteristics (p. 721) | html | pdf |
- Table 7.1.2. Software packages that allow extraction of reflection intensities including analysis of multiple profiles and calculation of error estimates (p. 726) | html | pdf |