International Tables for Crystallography (2006). Vol. F. ch. 12.1, pp. 247-255
https://doi.org/10.1107/97809553602060000679 |
Chapter 12.1. The preparation of heavy-atom derivatives of protein crystals for use in multiple isomorphous replacement and anomalous scattering
Contents
- 12.1. The preparation of heavy-atom derivatives of protein crystals for use in multiple isomorphous replacement and anomalous scattering (pp. 247-255) | html | pdf | chapter contents |
- 12.1.1. Introduction (p. 247) | html | pdf |
- 12.1.2. Heavy-atom data bank (pp. 247-248) | html | pdf |
- 12.1.3. Properties of heavy-atom compounds and their complexes (pp. 248-250) | html | pdf |
- 12.1.3.1. Stability (p. 248) | html | pdf |
- 12.1.3.2. Lability (p. 248) | html | pdf |
- 12.1.3.3. Oxidation state of metal ions in protein crystals (p. 248) | html | pdf |
- 12.1.3.4. Effect of pH (pp. 248-249) | html | pdf |
- 12.1.3.5. Effect of precipitants and buffers on heavy-atom binding (p. 249) | html | pdf |
- 12.1.3.6. Solubility of heavy-atom compounds (p. 249) | html | pdf |
- 12.1.3.7. Effect of concentration, time of soak and temperature on heavy-atom binding (p. 250) | html | pdf |
- 12.1.4. Amino acids as ligands (p. 250) | html | pdf |
- 12.1.5. Protein chemistry of heavy-atom reagents (pp. 250-254) | html | pdf |
- 12.1.5.1. Hard cations (p. 251) | html | pdf |
- 12.1.5.2. Thallium and lead ions (p. 251) | html | pdf |
- 12.1.5.3. B-metal reagents (pp. 251-253) | html | pdf |
- 12.1.5.4. Electrostatic binding of heavy-atom anions (p. 253) | html | pdf |
- 12.1.5.5. Hydrophobic heavy-atom reagents (pp. 253-254) | html | pdf |
- 12.1.5.6. Iodine (p. 254) | html | pdf |
- 12.1.5.7. Polynuclear reagents (p. 254) | html | pdf |
- 12.1.6. Metal-ion replacement in metalloproteins (pp. 254-255) | html | pdf |
- 12.1.7. Analogues of amino acids (p. 255) | html | pdf |
- 12.1.8. Use of the heavy-atom data bank to select derivatives (p. 255) | html | pdf |
- References | html | pdf |
- Figures
- Fig. 12.1.5.1. The binding site for uranyl ions in cytochrome b5 (oxidized: 3B5C) (p. 252) | html | pdf |
- Fig. 12.1.5.2. Mercuric ions replace zinc in thermolysin (3TLN) (p. 252) | html | pdf |
- Fig. 12.1.5.3. The binding of a silver ion to immunoglobulin Fab (2FB4) (p. 252) | html | pdf |
- Fig. 12.1.5.4. The binding of through a methionine in azurin (1AZU) (p. 252) | html | pdf |
- Fig. 12.1.5.5. The relative positions of methionine side chains (carbon: green; sulfur: yellow) in the parent crystals to the binding of platinum (pink) of (p. 252) | html | pdf |
- Fig. 12.1.5.6. The relative positions of cystine disulfide bridges (carbon: green; sulfur: yellow) in the parent crystals to the binding of platinum (pink) of (p. 253) | html | pdf |
- Fig. 12.1.5.7. The binding of to aldose dehydrogenase (8ADH) (p. 253) | html | pdf |
- Fig. 12.1.6.1. The displacement of calcium by samarium in thermolysin (p. 254) | html | pdf |
- Tables
- Table 12.1.3.1. Useful pH ranges of some heavy-atom reagents derived from the heavy-atom data bank (p. 249) | html | pdf |
- Table 12.1.5.1. The 23 most commonly used heavy-atom reagents (p. 251) | html | pdf |
- Table 12.1.5.2. The five most popular uranium derivatives (p. 251) | html | pdf |
- Table 12.1.5.3. The five most popular mercury derivatives (p. 251) | html | pdf |
- Table 12.1.5.4. The five most popular platinum derivatives (p. 253) | html | pdf |