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 Results for DC.creator="S." AND DC.creator="H." AND DC.creator="Hughes" in section 3.1.6 of volume F
Protein storage
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, Section 3.1.6.2, p. 89 [ doi:10.1107/97809553602060000810 ]
... glycerol. Both pH and ionic strength can affect a protein's tolerance to freezing and thawing. In many cases, buffer exchange ...

Assessment of sample homogeneity
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, Section 3.1.6.1, pp. 88-89 [ doi:10.1107/97809553602060000810 ]
... nature and origins of such subspecies below. Once the protein(s) is fractionated, either on an isoelectric focusing gel or on ... of mutations that improve solubility (Chapter 4.3 ). References Cohen, S. L., Ferre-D'Amare, A. R., Burley, S. K. & Chait, B. T. (1995). Probing the solution ...

Characterization of the purified product
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, Section 3.1.6, pp. 88-89 [ doi:10.1107/97809553602060000810 ]
... nature and origins of such subspecies below. Once the protein(s) is fractionated, either on an isoelectric focusing gel or on ... glycerol. Both pH and ionic strength can affect a protein's tolerance to freezing and thawing. In many cases, buffer exchange ... of how best to store it is not. References Cohen, S. L., Ferre-D'Amare, A. R., Burley, S. K. & ...

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