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 Results for DC.creator="D." AND DC.creator="Carvin" in section 12.1.3 of volume F
Properties of heavy-atom compounds and their complexes
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3, pp. 318-320 [ doi:10.1107/97809553602060000837 ]
... as or anions such as , and . The easily polarizable d electrons allow formation of covalent bonds with methionine, cysteine and ... 1968). Unpublished results. Gilliland, G. L., Tung, M., Blakeslee, D. M. & Ladner, J. E. (1994). Biological Macromolecular Crystallization Database ... J. Mol. Biol. 194, 705-712. Petsko, G. A., Phillips, D. C., Williams, R. J. P. & Wilson, I. A. (1978) ...

Solubility of heavy-atom compounds
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.6, pp. 319-320 [ doi:10.1107/97809553602060000837 ]
Solubility of heavy-atom compounds 12.1.3.6. Solubility of heavy-atom compounds The solubility of a heavy-atom compound will depend upon the precipitant, buffer and pH. Typically, the component present in the highest concentration is the precipitant, either as salts (e.g. ammonium sulfate) or as an organic-based reagent (e.g. ethanol ...

Effect of precipitants and buffers on heavy-atom binding
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.5, p. 319 [ doi:10.1107/97809553602060000837 ]
... be relatively unstable. References Gilliland, G. L., Tung, M., Blakeslee, D. M. & Ladner, J. E. (1994). Biological Macromolecular Crystallization Database ... data. Acta Cryst. D50, 408-413. Petsko, G. A., Phillips, D. C., Williams, R. J. P. & Wilson, I. A. (1978). ... J. Mol. Biol. 120, 345-359. Sigler, P. B. & Blow, D. M. (1965). A means of promoting heavy atom ...

Effect of pH
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.4, pp. 318-319 [ doi:10.1107/97809553602060000837 ]
Effect of pH 12.1.3.4. Effect of pH Although the pKa of an individual amino acid in solution is generally defined within narrow limits, environmental and steric factors give rise to a wide range of values in proteins. Thus, the hydrogen-ion concentration influences the thermodynamic and kinetic stability of potential complexes. ...

Oxidation state of metal ions in protein crystals
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.3, p. 318 [ doi:10.1107/97809553602060000837 ]
Oxidation state of metal ions in protein crystals 12.1.3.3. Oxidation state of metal ions in protein crystals In the environment of a living cell, the following oxidation states tend to be stable: References International Tables for Crystallography (2012). Vol. F, ch. 12.1, p. 318 International Union of Crystallography 2012 | home ...

Lability
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.2, p. 318 [ doi:10.1107/97809553602060000837 ]
... gold derivative might be investigated. References Petsko, G. A., Phillips, D. C., Williams, R. J. P. & Wilson, I. A. (1978). ...

Stability
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.1, p. 318 [ doi:10.1107/97809553602060000837 ]
... as or anions such as , and . The easily polarizable d electrons allow formation of covalent bonds with methionine, cysteine and ...

Effect of concentration, time of soak and temperature on heavy-atom binding
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.7, p. 320 [ doi:10.1107/97809553602060000837 ]
... temperature. References Blundell, T. L. (1968). Unpublished results. Ringe, D., Petsko, G. A., Yamakura, F., Suzuki, K. & Ohmori, D. (1983). Structure of iron superoxide dismutase from Pseudomonas ovalis ...

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