International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

© International Union of Crystallography 2006
International Tables for Crystallography (2006). Vol. F. ch. 19.4, p. 443   | 1 | 2 |

Section 19.4.6.2. Contrast matching

D. M. Engelmana* and P. B. Mooreb

aDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA, and  bDepartments of Chemistry and Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
Correspondence e-mail:  don@paradigm.csb.yale.edu

19.4.6.2. Contrast matching

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In some applications, use has been made of contrast matching a large part of a complex to study a component with a contrasting scattering density. Examples include studies of ribosomal proteins in situ (Nierhaus et al., 1983[link]; Nowotny et al., 1994[link]), proteins of the DNA-dependant RNA polymerase (Stöckel et al., 1980a[link]), studies of muscle proteins (Stone et al., 1998[link]) and a view of a membrane protein in a lipid bilayer (Hunt et al., 1997[link]).

References

First citation Hunt, J. F., McCrea, P. D., Zaccai, G. & Engelman, D. M. (1997). Assessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering. J. Mol. Biol. 273, 1004–1019.Google Scholar
 First citation Nierhaus, K. H., Lietzke, R., May, R. P., Nowotny, V., Schulze, H., Simpson, K., Wurmbach, P. & Stuhrmann, H. B. (1983). Shape determinations of ribosomal proteins in situ. Proc. Natl Acad. Sci. USA, 80, 2889–2893.Google Scholar
 First citation Nowotny, P., Ruhl, M., Nowotny, V., May, R. P., Burkhardt, N., Voss, H. & Nierhaus, K. H. (1994). Direct shape determination of ribosomal proteins in solution and within the ribosome by means of neutron scattering. Biophys. Chem. 53, 115–122.Google Scholar
 First citation Stone, D. B., Timmins, P. A., Schneider, D. K., Krylova, I., Ramos, C. H., Reinach, F. C. & Mendelson, R. A. (1998). The effect of regulatory Ca2+ on the in situ structures of troponin C and troponin I: a neutron scattering study. J. Mol. Biol. 281, 689–704.Google Scholar
 First citation Stöckel, P., May, R., Strell, I., Cejka, Z., Hoppe, W., Heumann, H., Zillig, W. & Crespi, H. (1980a). The core subunit structure in RNA polymerase holoenzyme determined by neutron small-angle scattering. Eur. J. Biochem. 112, 411–417.Google Scholar








































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