modify your search
 Results for DC.creator="S." AND DC.creator="H." AND DC.creator="Hughes"
Preparing recombinant proteins for X-ray crystallography
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, ch. 3.1, pp. 75-91 [ doi:10.1107/97809553602060000810 ]
... those offered by Cold Spring Harbor Laboratory), meetings (i.e. IBC's International Conference on Expression Technologies, Washington DC, 1997) and a ... RNA intermediate, thus removing unwanted introns (Shimotohno & Temin, 1982; Sorge & Hughes, 1982). If a good sequence is not available, one ... cassette mutagenesis using Bsp MI or a related enzyme; Boyer & Hughes, 1996). Ordinarily, however, these alternative strategies are only ...

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 ...
     [more results from section 3.1.6 in volume F]

Purifying and refolding denatured proteins
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, Section 3.1.5.3, pp. 87-88 [ doi:10.1107/97809553602060000810 ]
... bodies. Biotechnol. Bioeng. 41, 3-13. Guise, A. D., West, S. M. & Chaudhuri, J. B. (1996). Protein folding in vivo ... Anal. Biochem. 230, 8-15. Krueger, J. K., Kulke, M. H., Schutt, C. & Stock, J. (1989). Protein inclusion body formation ... and inclusion body formation. Biotechnology, 7, 690-697. Werner, M. H., Clore, G. M., Gronenborn, A. M., Kondoh, A. & Fisher, ...
     [more results from section 3.1.5 in volume F]

Mammalian cells
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, Section 3.1.4.4, pp. 84-85 [ doi:10.1107/97809553602060000810 ]
... antibody. Nature (London), 393, 648-659. Rossi, F. M. & Blau, H. M. (1998). Recent advances in inducible expression systems. Curr. ...
     [more results from section 3.1.4 in volume F]

Addition of tags or domains
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, Section 3.1.3.3, p. 77 [ doi:10.1107/97809553602060000810 ]
... CBP), cellulose-binding domain (CBD), chitin-binding domain (CBD), glutathione S-transferase (GST), maltose-binding protein (MBP), protein A domains, ribonuclease A S-peptide (S-tag) and thioridazine (Trx)] have already been engineered into ...
     [more results from section 3.1.3 in volume F]

Overview
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, Section 3.1.2, pp. 75-76 [ doi:10.1107/97809553602060000810 ]
Overview 3.1.2. Overview The idea that underlies the problem of expressing large amounts of a recombinant protein is straightforward: prepare a DNA segment that, when introduced into an appropriate host, will cause the abundant expression of the relevant protein. However, as the saying goes, `The devil is in the details.' Not ...

Introduction
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, Section 3.1.1, p. 75 [ doi:10.1107/97809553602060000810 ]
... those offered by Cold Spring Harbor Laboratory), meetings (i.e. IBC's International Conference on Expression Technologies, Washington DC, 1997) and a ... Associates and Wiley. Bollag, D. M., Rozycki, M. D. & Edelstein, S. J. (1996). Protein Methods. New York: Wiley-Liss. Sambrook ...

Reprise
Hughes, S. H. and Stock, A. M.  International Tables for Crystallography (2012). Vol. F, Section 3.1.7, pp. 89-90 [ doi:10.1107/97809553602060000810 ]
Reprise 3.1.7. Reprise We have reached a point where it is possible to use recombinant DNA techniques to produce most proteins in quantities sufficient for crystallography. Both high-level expression systems and methods for making defined modifications of recombinant proteins vastly simplify the process of purification. This has played a direct ...

powered by swish-e
























































to end of page
to top of page