International Tables for Crystallography (2012). Vol. F, ch. 19.3, pp. 563-574   | 1 | 2 |
doi: 10.1107/97809553602060000869

Chapter 19.3. Small-angle X-ray scattering

Contents

  • 19.3. Small-angle X-ray scattering  (pp. 563-574) | html | pdf | chapter contents |
    • 19.3.1. Introduction  (p. 563) | html | pdf |
    • 19.3.2. Small-angle single-crystal X-ray diffraction studies  (pp. 563-564) | html | pdf |
    • 19.3.3. Solution X-ray scattering studies  (pp. 564-573) | html | pdf |
      • 19.3.3.1. Information content of solution scattering  (pp. 564-568) | html | pdf |
        • 19.3.3.1.1. Solution scattering and crystal structures  (p. 567) | html | pdf |
        • 19.3.3.1.2. Low-resolution model determination using solution scattering  (pp. 567-568) | html | pdf |
      • 19.3.3.2. Instrumentation for small-angle X-ray scattering  (pp. 568-569) | html | pdf |
        • 19.3.3.2.1. Instruments on conventional sources  (p. 568) | html | pdf |
        • 19.3.3.2.2. Synchrotron instruments  (pp. 568-569) | html | pdf |
      • 19.3.3.3. Experimental considerations  (pp. 569-571) | html | pdf |
        • 19.3.3.3.1. Sample preparation  (p. 569) | html | pdf |
        • 19.3.3.3.2. Sample-handling devices  (pp. 569-570) | html | pdf |
        • 19.3.3.3.3. Designing experiments  (p. 570) | html | pdf |
        • 19.3.3.3.4. Data-collection practices  (pp. 570-571) | html | pdf |
        • 19.3.3.3.5. Data processing and analysis  (p. 571) | html | pdf |
      • 19.3.3.4. Recent applications of solution X-ray scattering in structural molecular biology  (pp. 571-573) | html | pdf |
        • 19.3.3.4.1. Studies of proteins in solution that complement high-resolution structures  (pp. 571-572) | html | pdf |
        • 19.3.3.4.2. Time-resolved studies  (p. 572) | html | pdf |
        • 19.3.3.4.3. Protein-folding studies  (pp. 572-573) | html | pdf |
    • Figures
      • Fig. 19.3.2.1. A cross section of the electron-density map of sFHV at 14 Å resolution  (p. 563) | html | pdf |
      • Fig. 19.3.2.2. Comparison of the absolute values of single-crystal reflection amplitudes (circles), the solution scattering intensity (thick curve) and the calculated scattering intensity from a uniform sphere (thin curve)  (p. 564) | html | pdf |
      • Fig. 19.3.3.1. Definition of electron-density contrast  (p. 565) | html | pdf |
      • Fig. 19.3.3.2. ( a ) The calculated solution X-ray scattering curves from the crystal structure of Salmonella typhimorium glutamine synthetase  (p. 565) | html | pdf |
      • Fig. 19.3.3.3. ( a ) Interparticle interference in biological small-angle scattering  (p. 566) | html | pdf |
      • Fig. 19.3.3.4. Definition of the electron pair distance distribution function [P({\bf r})]  (p. 567) | html | pdf |
      • Fig. 19.3.3.5. A small-angle X-ray scattering instrument on BL 4–2 at the Stanford Synchrotron Radiation Laboratory  (p. 568) | html | pdf |
      • Fig. 19.3.3.6. ( a ) Flat-window cells for solution scattering and ( b ) a diagram of a stopped-flow rapid mixer for time-resolved solution scattering  (p. 570) | html | pdf |
    • Tables
      • Table 19.3.3.1. List of commonly used software for solution scattering  (p. 571) | html | pdf |