(International Tables) Crystallography of biological macromolecules

International Tables for Crystallography
Volume F: Crystallography of biological macromolecules

First online edition (2006) ISBN: 978-0-7923-6857-1 eISBN: 978-1-4020-5416-7 doi: 10.1107/97809553602060000106

Edited by M. G. Rossmann and E. Arnold

Preface (p. xxiii) | html | pdf |
E. Arnold and M. G. Rossmann

Part 1. Introduction
- 1.1. Overview (pp. 1-3) | html | pdf | chapter contents |
  E. Arnold and M. G. Rossmann
- 1.2. Historical background (pp. 4-9) | html | pdf | chapter contents |
  M. G. Rossmann
  - 1.2.1. Introduction (p. 4) | html | pdf |
  - 1.2.2. 1912 to the 1950s (pp. 4-5) | html | pdf |
  - 1.2.3. The first investigations of biological macromolecules (p. 5) | html | pdf |
  - 1.2.4. Globular proteins in the 1950s (pp. 5-7) | html | pdf |
  - 1.2.5. The first protein structures (1957 to the 1970s) (pp. 7-8) | html | pdf |
  - 1.2.6. Technological developments (1958 to the 1980s) (pp. 8-9) | html | pdf |
  - 1.2.7. Meetings (p. 9) | html | pdf |
  - References | html | pdf |
  - Figures
    - Fig. 1.2.4.1. Change of structure amplitude for horse haemoglobin as a function of salt concentration in the suspension medium of the low-order h 0 l reflections at various lattice shrinkage stages (C, C′, D, E, F, G, H, J) (p. 6) | html | pdf |
    - Fig. 1.2.5.1. A model of the myoglobin molecule at 6 Å resolution (p. 7) | html | pdf |
    - Fig. 1.2.5.2. Cylindrical sections through a helical segment of a myoglobin polypeptide chain (p. 7) | html | pdf |
    - Fig. 1.2.6.1. The 2 Å-resolution map of sperm-whale myoglobin was represented by coloured Meccano-set clips on a forest of vertical rods (p. 8) | html | pdf |
- 1.3. Macromolecular crystallography and medicine (pp. 10-25) | html | pdf | chapter contents |
  W. G. J. Hol and C. L. M. J. Verlinde
  - 1.3.1. Introduction (p. 10) | html | pdf |
  - 1.3.2. Crystallography and medicine (pp. 10-11) | html | pdf |
  - 1.3.3. Crystallography and genetic diseases (pp. 11-12) | html | pdf |
  - 1.3.4. Crystallography and development of novel pharmaceuticals (pp. 12-24) | html | pdf |
    - 1.3.4.1. Infectious diseases (pp. 13-15) | html | pdf |
      - 1.3.4.1.1. Viral diseases (p. 13) | html | pdf |
      - 1.3.4.1.2. Bacterial diseases (p. 13) | html | pdf |
      - 1.3.4.1.3. Protozoan infections (pp. 13-15) | html | pdf |
      - 1.3.4.1.4. Fungi (p. 15) | html | pdf |
      - 1.3.4.1.5. Helminths (p. 15) | html | pdf |
    - 1.3.4.2. Resistance (pp. 15-21) | html | pdf |
    - 1.3.4.3. Non-communicable diseases (pp. 21-24) | html | pdf |
      - 1.3.4.3.1. Cancers (p. 21) | html | pdf |
      - 1.3.4.3.2. Diabetes (p. 21) | html | pdf |
      - 1.3.4.3.3. Blindness (p. 21) | html | pdf |
      - 1.3.4.3.4. Cardiovascular disorders (p. 21) | html | pdf |
      - 1.3.4.3.5. Neurological disorders (p. 24) | html | pdf |
    - 1.3.4.4. Drug metabolism and crystallography (p. 24) | html | pdf |
    - 1.3.4.5. Drug manufacturing and crystallography (p. 24) | html | pdf |
  - 1.3.5. Vaccines, immunology and crystallography (pp. 24-25) | html | pdf |
  - 1.3.6. Outlook and dreams (p. 25) | html | pdf |
  - References | html | pdf |
  - Figures
    - Fig. 1.3.4.1. The structure-based drug design cycle (p. 13) | html | pdf |
  - Tables
    - Table 1.3.3.1. Crystal structures and genetic diseases (p. 11) | html | pdf |
    - Table 1.3.4.1. Important human pathogenic viruses and their proteins (pp. 14-15) | html | pdf |
    - Table 1.3.4.2. Protein structures of important human pathogenic bacteria (pp. 16-18) | html | pdf |
    - Table 1.3.4.3. Protein structures of important human pathogenic protozoa, fungi and helminths (pp. 19-20) | html | pdf |
    - Table 1.3.4.4. Mechanisms of resistance (p. 20) | html | pdf |
    - Table 1.3.4.5. Important human protein structures in drug design (pp. 22-23) | html | pdf |
- 1.4. Perspectives for the future (pp. 26-43) | html | pdf | chapter contents |
  E. Arnold and M. G. Rossmann
  - 1.4.1. Gazing into the crystal ball (pp. 26-27) | html | pdf |
    E. Arnold
    - 1.4.1.1. What can we expect to see in the future of science and technology in general? (p. 26) | html | pdf |
    - 1.4.1.2. How will crystallography change in the future? (pp. 26-27) | html | pdf |
  - 1.4.2. Brief comments on Gazing into the crystal ball (p. 27) | html | pdf |
    M. G. Rossmann

Part 2. Basic crystallography
- 2.1. Introduction to basic crystallography (pp. 45-63) | html | pdf | chapter contents |
  J. Drenth
  - 2.1.1. Crystals (pp. 45-46) | html | pdf |
  - 2.1.2. Symmetry (pp. 46-47) | html | pdf |
  - 2.1.3. Point groups and crystal systems (pp. 47-52) | html | pdf |
  - 2.1.4. Basic diffraction physics (pp. 52-57) | html | pdf |
    - 2.1.4.1. Diffraction by one electron (pp. 52-53) | html | pdf |
    - 2.1.4.2. Scattering by a system of two electrons (p. 53) | html | pdf |
    - 2.1.4.3. Scattering by atoms (pp. 53-54) | html | pdf |
      - 2.1.4.3.1. Scattering by one atom (pp. 53-54) | html | pdf |
      - 2.1.4.3.2. Scattering by a plane of atoms (p. 54) | html | pdf |
    - 2.1.4.4. Anomalous dispersion (pp. 54-55) | html | pdf |
    - 2.1.4.5. Scattering by a crystal (pp. 55-56) | html | pdf |
    - 2.1.4.6. The structure factor (pp. 56-57) | html | pdf |
  - 2.1.5. Reciprocal space and the Ewald sphere (pp. 57-58) | html | pdf |
  - 2.1.6. Mosaicity and integrated reflection intensity (pp. 58-59) | html | pdf |
  - 2.1.7. Calculation of electron density (pp. 59-60) | html | pdf |
  - 2.1.8. Symmetry in the diffraction pattern (pp. 60-61) | html | pdf |
  - 2.1.9. The Patterson function (pp. 61-62) | html | pdf |
  - References | html | pdf |
  - Figures
    - Fig. 2.1.1.1. One unit cell with axes a , b and c (p. 45) | html | pdf |
    - Fig. 2.1.1.2. A set of $[5 \times 3 \times 3]$ unit cells (p. 45) | html | pdf |
    - Fig. 2.1.1.3. A two-dimensional lattice with $[3 \times 3]$ unit cells (p. 46) | html | pdf |
    - Fig. 2.1.1.4. Non-centred and centred unit cells (p. 46) | html | pdf |
    - Fig. 2.1.3.1. How to construct a stereographic projection (p. 47) | html | pdf |
    - Fig. 2.1.3.2. A rhombohedral unit cell (p. 47) | html | pdf |
    - Fig. 2.1.3.3. The 14 Bravais lattices (p. 52) | html | pdf |
    - Fig. 2.1.4.1. The electric vector of a monochromatic and polarized X-ray beam is in the plane (p. 53) | html | pdf |
    - Fig. 2.1.4.2. The black dots are electrons (p. 53) | html | pdf |
    - Fig. 2.1.4.3. The direction of the incident wave is indicated by $[{\bf s}_{o}]$ and that of the scattered wave by s (p. 53) | html | pdf |
    - Fig. 2.1.4.4. An Argand diagram for the scattering by two electrons (p. 54) | html | pdf |
    - Fig. 2.1.4.5. The atomic scattering factor f for carbon as a function of $[\sin \theta /\lambda]$ , expressed in units of the scattering by one electron (p. 54) | html | pdf |
    - Fig. 2.1.4.6. S is the X-ray source and D is the detector (p. 54) | html | pdf |
    - Fig. 2.1.4.7. Schematic picture of the Argand diagram for the scattering by atoms in a plane (p. 55) | html | pdf |
    - Fig. 2.1.4.8. The atomic scattering factor as a vector in the Argand diagram (p. 55) | html | pdf |
    - Fig. 2.1.4.9. X-ray diffraction by a crystal is, in Bragg's conception, reflection by lattice planes (p. 56) | html | pdf |
    - Fig. 2.1.4.10. The Wilson plot for phospholipase A ₂ with data to 1.7 Å resolution (p. 57) | html | pdf |
    - Fig. 2.1.5.1. A two-dimensional real unit cell is drawn together with its reciprocal unit cell (p. 58) | html | pdf |
    - Fig. 2.1.5.2. The circle is, in fact, a sphere with radius $[1/\lambda]$ (p. 58) | html | pdf |
    - Fig. 2.1.7.1. An Argand diagram for the structure factors of the two members of a Friedel pair (p. 60) | html | pdf |
    - Fig. 2.1.9.1. ( a ) A two-dimensional unit cell with two atoms (p. 62) | html | pdf |
  - Tables
    - Table 2.1.2.1. The most common space groups for protein crystals (p. 46) | html | pdf |
    - Table 2.1.3.1. The 11 enantiomorphic point groups (pp. 48-49) | html | pdf |
    - Table 2.1.3.2. The 11 point groups with a centre of symmetry (pp. 50-51) | html | pdf |
    - Table 2.1.3.3. The icosahedral point group 532 (p. 51) | html | pdf |
    - Table 2.1.3.4. The seven crystal systems (p. 52) | html | pdf |
    - Table 2.1.4.1. The position of the K α edge of different elements (p. 54) | html | pdf |

Part 3. Techniques of molecular biology
- 3.1. Preparing recombinant proteins for X-ray crystallography (pp. 65-80) | html | pdf | chapter contents |
  S. H. Hughes and A. M. Stock
  - 3.1.1. Introduction (p. 65) | html | pdf |
  - 3.1.2. Overview (p. 65) | html | pdf |
  - 3.1.3. Engineering an expression construct (pp. 66-67) | html | pdf |
    - 3.1.3.1. Choosing an expression system (p. 66) | html | pdf |
    - 3.1.3.2. Creating an expression construct (p. 66) | html | pdf |
    - 3.1.3.3. Addition of tags or domains (p. 67) | html | pdf |
  - 3.1.4. Expression systems (pp. 67-74) | html | pdf |
    - 3.1.4.1. E. coli (pp. 67-71) | html | pdf |
    - 3.1.4.2. Yeast (pp. 71-72) | html | pdf |
    - 3.1.4.3. Baculoviruses and insect cells (pp. 72-73) | html | pdf |
    - 3.1.4.4. Mammalian cells (pp. 73-74) | html | pdf |
  - 3.1.5. Protein purification (pp. 75-77) | html | pdf |
    - 3.1.5.1. Conventional protein purification (pp. 75-76) | html | pdf |
    - 3.1.5.2. Affinity purification (pp. 76-77) | html | pdf |
    - 3.1.5.3. Purifying and refolding denatured proteins (p. 77) | html | pdf |
  - 3.1.6. Characterization of the purified product (pp. 77-78) | html | pdf |
    - 3.1.6.1. Assessment of sample homogeneity (pp. 77-78) | html | pdf |
    - 3.1.6.2. Protein storage (p. 78) | html | pdf |
  - 3.1.7. Reprise (pp. 78-79) | html | pdf |
  - References | html | pdf |
  - Figures
    - Fig. 3.1.3.1. Creating an expression construct (p. 67) | html | pdf |
    - Fig. 3.1.5.1. Protein purification strategy (p. 75) | html | pdf |
  - Tables
    - Table 3.1.4.1. Strategies for improving expression in E. coli (p. 68) | html | pdf |

Part 4. Crystallization
- 4.1. General methods (pp. 81-93) | html | pdf | chapter contents |
  R. Giegé and A. McPherson
  - 4.1.1. Introduction (p. 81) | html | pdf |
  - 4.1.2. Crystallization arrangements and methodologies (pp. 81-86) | html | pdf |
    - 4.1.2.1. General considerations (p. 81) | html | pdf |
    - 4.1.2.2. Batch crystallizations (pp. 81-82) | html | pdf |
    - 4.1.2.3. Dialysis methods (p. 82) | html | pdf |
    - 4.1.2.4. Vapour diffusion methods (pp. 82-84) | html | pdf |
    - 4.1.2.5. Interface diffusion and the gel acupuncture method (p. 84) | html | pdf |
    - 4.1.2.6. Crystallization in gelled media (pp. 84-86) | html | pdf |
    - 4.1.2.7. Miscellaneous crystallization methods (p. 86) | html | pdf |
    - 4.1.2.8. Seeding (p. 86) | html | pdf |
  - 4.1.3. Parameters that affect crystallization of macromolecules (pp. 86-88) | html | pdf |
    - 4.1.3.1. Crystallizing agents (pp. 86-87) | html | pdf |
    - 4.1.3.2. Other chemical, physical and biochemical variables (pp. 87-88) | html | pdf |
    - 4.1.3.3. Additives (p. 88) | html | pdf |
  - 4.1.4. How to crystallize a new macromolecule (pp. 88-89) | html | pdf |
    - 4.1.4.1. Rules and general principles (p. 88) | html | pdf |
    - 4.1.4.2. Purity and homogeneity (p. 88) | html | pdf |
    - 4.1.4.3. Sample preparation (pp. 88-89) | html | pdf |
    - 4.1.4.4. Strategic concerns: a summary (p. 89) | html | pdf |
  - 4.1.5. Techniques for physical characterization of crystallization (pp. 89-91) | html | pdf |
    - 4.1.5.1. Techniques for studying prenucleation and nucleation (pp. 89-90) | html | pdf |
    - 4.1.5.2. Techniques for studying growth mechanisms (pp. 90-91) | html | pdf |
    - 4.1.5.3. Techniques for evaluating crystal perfection (p. 91) | html | pdf |
  - 4.1.6. Use of microgravity (pp. 91-93) | html | pdf |
    - 4.1.6.1. Why microgravity? (p. 91) | html | pdf |
    - 4.1.6.2. Instrumentation (p. 91) | html | pdf |
    - 4.1.6.3. Present results: a summary (pp. 91-92) | html | pdf |
    - 4.1.6.4. Interpretation of data (pp. 92-93) | html | pdf |
    - 4.1.6.5. The future of crystallization under microgravity (p. 93) | html | pdf |
  - References | html | pdf |
  - Figures
    - Fig. 4.1.2.1. Principles of the major methods currently used to crystallize biological macromolecules (p. 82) | html | pdf |
    - Fig. 4.1.2.2. Two versions of boxes for vapour diffusion crystallization (p. 83) | html | pdf |
    - Fig. 4.1.2.3. Principle of the gel acupuncture method for the crystallization of proteins by counter-diffusion (p. 84) | html | pdf |
    - Fig. 4.1.5.1. Visualization of the surface of yeast tRNA ^Phe crystals by AFM (p. 90) | html | pdf |
  - Tables
    - Table 4.1.2.1. Factors affecting crystallization (p. 83) | html | pdf |
    - Table 4.1.2.2. Crystallizing agents for protein crystallization (pp. 85-86) | html | pdf |
- 4.2. Crystallization of membrane proteins (pp. 94-99) | html | pdf | chapter contents |
  H. Michel
  - 4.2.1. Introduction (p. 94) | html | pdf |
  - 4.2.2. Principles of membrane-protein crystallization (p. 94) | html | pdf |
  - 4.2.3. General properties of detergents relevant to membrane-protein crystallization (pp. 94-98) | html | pdf |
  - 4.2.4. The `small amphiphile concept' (p. 98) | html | pdf |
  - 4.2.5. Membrane-protein crystallization with the help of antibody Fv fragments (pp. 98-99) | html | pdf |
  - 4.2.6. Membrane-protein crystallization using cubic bicontinuous lipidic phases (p. 99) | html | pdf |
  - 4.2.7. General recommendations (p. 99) | html | pdf |
  - References | html | pdf |
  - Tables
    - Table 4.2.1.1. Compilation of membrane proteins with known structures, including crystallization conditions and key references for the structure determinations (pp. 95-96) | html | pdf |
    - Table 4.2.2.1. Potentially useful detergents for membrane-protein crystallizations with molecular weights and CMCs [in water, from Michel (1991) or as provided by the vendor] (p. 97) | html | pdf |
    - Table 4.2.3.1. Summary of the results of attempts to crystallize the two-subunit cytochrome c oxidase from the soil bacterium Paracoccus denitrificans using different detergents (after Ostermeier et al. , 1997) (p. 98) | html | pdf |
- 4.3. Application of protein engineering to improve crystal properties (pp. 100-110) | html | pdf | chapter contents |
  D. R. Davies and A. Burgess Hickman
  - 4.3.1. Introduction (p. 100) | html | pdf |
  - 4.3.2. Improving solubility (pp. 100-101) | html | pdf |
  - 4.3.3. Use of fusion proteins (p. 101) | html | pdf |
  - 4.3.4. Mutations to accelerate crystallization (p. 101) | html | pdf |
  - 4.3.5. Mutations to improve diffraction quality (pp. 101-102) | html | pdf |
  - 4.3.6. Avoiding protein heterogeneity (p. 102) | html | pdf |
  - 4.3.7. Engineering crystal contacts to enhance crystallization in a particular crystal form (pp. 102-103) | html | pdf |
  - 4.3.8. Engineering heavy-atom sites (p. 103) | html | pdf |
  - References | html | pdf |

Part 5. Crystal properties and handling
- 5.1. Crystal morphology, optical properties of crystals and crystal mounting (pp. 111-116) | html | pdf | chapter contents |
  H. L. Carrell and J. P. Glusker
  - 5.1.1. Crystal morphology and optical properties (pp. 111-114) | html | pdf |
    - 5.1.1.1. Crystal growth habits (pp. 111-112) | html | pdf |
      - 5.1.1.1.1. The shape of a crystal – growth habits (p. 111) | html | pdf |
      - 5.1.1.1.2. Quality of protein crystals (p. 111) | html | pdf |
      - 5.1.1.1.3. Polymorphism (pp. 111-112) | html | pdf |
      - 5.1.1.1.4. Twinning (p. 112) | html | pdf |
    - 5.1.1.2. Properties of crystal faces (pp. 112-113) | html | pdf |
      - 5.1.1.2.1. Indexing crystal faces (pp. 112-113) | html | pdf |
      - 5.1.1.2.2. Measurement of crystal habit (p. 113) | html | pdf |
    - 5.1.1.3. Optical properties (p. 113) | html | pdf |
      - 5.1.1.3.1. Crystals between crossed polarizers (p. 113) | html | pdf |
      - 5.1.1.3.2. Refractive indices and what they tell us about structure (p. 113) | html | pdf |
    - 5.1.1.4. Packing of molecules in crystals (p. 114) | html | pdf |
  - 5.1.2. Crystal mounting (pp. 114-116) | html | pdf |
    - 5.1.2.1. Introduction to crystal mounting (p. 114) | html | pdf |
    - 5.1.2.2. Tools for crystal mounting (pp. 114-115) | html | pdf |
      - 5.1.2.2.1. Microscope (p. 114) | html | pdf |
      - 5.1.2.2.2. Capillaries (pp. 114-115) | html | pdf |
      - 5.1.2.2.3. Thumb pump (p. 115) | html | pdf |
      - 5.1.2.2.4. Heater (p. 115) | html | pdf |
    - 5.1.2.3. Capillary mounting (pp. 115-116) | html | pdf |
  - References | html | pdf |
  - Figures
    - Fig. 5.1.1.1. Crystal faces (p. 112) | html | pdf |
    - Fig. 5.1.2.1. Tools commonly used for mounting crystals (p. 114) | html | pdf |
    - Fig. 5.1.2.2. Mounting a crystal in a capillary (p. 115) | html | pdf |
- 5.2. Crystal-density measurements (pp. 117-123) | html | pdf | chapter contents |
  E. M. Westbrook
  - 5.2.1. Introduction (p. 117) | html | pdf |
  - 5.2.2. Solvent in macromolecular crystals (p. 117) | html | pdf |
  - 5.2.3. Matthews number (p. 117) | html | pdf |
  - 5.2.4. Algebraic concepts (pp. 117-118) | html | pdf |
  - 5.2.5. Experimental estimation of hydration (p. 118) | html | pdf |
  - 5.2.6. Methods for measuring crystal density (pp. 118-121) | html | pdf |
    - 5.2.6.1. Pycnometry (pp. 118-119) | html | pdf |
    - 5.2.6.2. Volumenometry (p. 119) | html | pdf |
    - 5.2.6.3. The method of Archimedes (p. 119) | html | pdf |
    - 5.2.6.4. Immersion microbalance (p. 119) | html | pdf |
    - 5.2.6.5. Flotation (p. 119) | html | pdf |
    - 5.2.6.6. Tomographic crystal-volume measurement (pp. 119-120) | html | pdf |
    - 5.2.6.7. Gradient-tube method (pp. 120-121) | html | pdf |
  - 5.2.7. How to handle the solvent density (p. 121) | html | pdf |
  - References | html | pdf |
  - Tables
    - Table 5.2.6.1. Organic liquids for density determinations (p. 120) | html | pdf |
    - Table 5.2.6.2. Inorganic salts for density determinations (p. 120) | html | pdf |

Part 6. Radiation sources and optics
- 6.1. X-ray sources (pp. 125-132) | html | pdf | chapter contents |
  U. W. Arndt
  - 6.1.1. Overview (p. 125) | html | pdf |
  - 6.1.2. Generation of X-rays (pp. 125-127) | html | pdf |
    - 6.1.2.1. Stationary-target X-ray tubes (p. 125) | html | pdf |
    - 6.1.2.2. Rotating-anode X-ray tubes (pp. 125-126) | html | pdf |
    - 6.1.2.3. Microfocus X-ray tubes (p. 126) | html | pdf |
    - 6.1.2.4. Synchrotron-radiation sources (pp. 126-127) | html | pdf |
  - 6.1.3. Properties of the X-ray beam (pp. 127-129) | html | pdf |
    - 6.1.3.1. Beam size (p. 128) | html | pdf |
    - 6.1.3.2. X-ray wavelength (p. 128) | html | pdf |
    - 6.1.3.3. Spectral composition (p. 128) | html | pdf |
    - 6.1.3.4. Intensity (pp. 128-129) | html | pdf |
    - 6.1.3.5. Cross fire (p. 129) | html | pdf |
    - 6.1.3.6. Beam stability (p. 129) | html | pdf |
  - 6.1.4. Beam conditioning (pp. 129-132) | html | pdf |
    - 6.1.4.1. X-ray mirrors (pp. 129-131) | html | pdf |
    - 6.1.4.2. Focusing collimators for microfocus sources (p. 131) | html | pdf |
    - 6.1.4.3. Other focusing collimators (p. 131) | html | pdf |
    - 6.1.4.4. Crystal monochromators (pp. 131-132) | html | pdf |
  - References | html | pdf |
  - Figures
    - Fig. 6.1.2.1. Section through a sealed X-ray tube (p. 125) | html | pdf |
    - Fig. 6.1.2.2. Synchrotron radiation emitted by a relativistic electron travelling in a curved trajectory (p. 126) | html | pdf |
    - Fig. 6.1.2.3. Comparison of the spectra from the storage ring SPEAR (p. 127) | html | pdf |
    - Fig. 6.1.2.4. Main components of a dedicated electron storage-ring synchrotron-radiation source (p. 127) | html | pdf |
    - Fig. 6.1.2.5. Electron trajectory within a multipole wiggler or undulator (p. 127) | html | pdf |
    - Fig. 6.1.2.6. Spectral distribution and critical wavelengths for ( a ) a dipole magnet, ( b ) a wavelength shifter and ( c ) a multipole wiggler at the ESRF (p. 128) | html | pdf |
    - Fig. 6.1.4.1. Production of a point focus by successive reflections at two orthogonal curved mirrors (p. 130) | html | pdf |
    - Fig. 6.1.4.2. The `catamegonic' arrangement of Montel (1957), in which two confocal mirrors with orthogonal curvatures lie side-by-side (p. 130) | html | pdf |
    - Fig. 6.1.4.3. Mirror bender (after Franks, 1955) (p. 130) | html | pdf |
    - Fig. 6.1.4.4. Triangular mirror bender as described by Lemonnier et al (p. 130) | html | pdf |
    - Fig. 6.1.4.5. Mirror holder with machined slots for two orthogonal pairs of curved mirrors (after Arndt, Duncumb et al (p. 130) | html | pdf |
    - Fig. 6.1.4.6. Ellipsoidal mirror for use with a microfocus X-ray tube, where x ₁ is ∼15 mm (p. 131) | html | pdf |
    - Fig. 6.1.4.7. A polycapillary collimator (after Bly & Gibson, 1996) (p. 131) | html | pdf |
  - Tables
    - Table 6.1.2.1. Standard X-ray tube inserts (p. 125) | html | pdf |
- 6.2. Neutron sources (pp. 133-142) | html | pdf | chapter contents |
  B. P. Schoenborn and R. Knott
  - 6.2.1. Reactors (pp. 133-137) | html | pdf |
    - 6.2.1.1. Basic reactor physics (p. 133) | html | pdf |
    - 6.2.1.2. Moderators for neutron scattering (pp. 133-134) | html | pdf |
      - 6.2.1.2.1. Thermal moderators (p. 134) | html | pdf |
      - 6.2.1.2.2. Cold moderators (p. 134) | html | pdf |
    - 6.2.1.3. Beamline components (pp. 134-136) | html | pdf |
      - 6.2.1.3.1. Collimators and filters (p. 135) | html | pdf |
      - 6.2.1.3.2. Crystal monochromators (p. 135) | html | pdf |
      - 6.2.1.3.3. Multilayer monochromators and supermirrors (pp. 135-136) | html | pdf |
      - 6.2.1.3.4. Velocity selectors (p. 136) | html |

International Tables for CrystallographyVolume F: Crystallography of biological macromolecules

Edited by M. G. Rossmann and E. Arnold

Contents

International Tables for Crystallography
Volume F: Crystallography of biological macromolecules