Abstract
X-ray crystallography provides one of the most important tools for understanding structure-function relationships in proteins. Over the last several years, the scientific community has accumulated a great deal of experience making crystals and solving protein structures by X-ray diffraction. However, often the X-ray approach cannot be used because of the failure to obtain crystals, which is still considered as the single greatest experimental problem in crystallography. Currently, there is no method for predicting the conditions needed to obtain crystals for a given protein. Researchers simply screen a large number of conditions hoping to find crystals in any of the trials. Given crystals under one set of conditions, even crystals of low quality, conditions in the neighborhood of the successful trial are again surveyed in hopes of finding conditions for obtaining improved crystals. Even though crystals are obtained, some are not suitable for structure determination by X-ray diffraction. The first requirement is that a crystal must contain a sufficiently high degree of order relating one molecule to another over a sufficient number of molecules. In addition, a crystal must have an appropriate size and shape. Needle-like crystals are of insufficient size in two dimensions and may require application of seeding techniques using initial crystals as nuclei for larger crystals, but it is often not a straightforward procedure.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Maclennan, D. H. and Wong, P. T. (1971) Isolation of a calcium-sequestering protein from sarcoplasmic reticulum. Proc. Natl. Acad. Sci. USA 68, 1231–1235.
Yano, K. and Zarain-Herzberg, A. (1994) Sarcoplasmic reticulum calsequestrins: structural and functional properties. Mol. Cell Biochem. 135, 61–70.
Williams R. W. and Beeler, T. J. (1986) Secondary structure of calsequestrin in solutions and in crystals as determined by Raman spectroscopy. J. Biol. Chem. 261, 12,408–12,413.
Maurer, A., Tanaka, M. Ozawa, T., and Fleischer, S. (1985) Purification and crystallization of the calcium binding protein of sarcoplasmic reticulum from skeletal muscle. Proc. Nat. Acad. Sci. USA 82, 4036–4040.
Hayakawa, K., Swenson, L., Baksn, S., Wei, Y., Michalak, M., and Derewenda, Z. S.(1994) Crystallization of canine cardiac calsequestrin. J. Mol. Biol. 235, 357–360.
Wang, S., Trumble, B., Liao, H., Dunker, K., and Kang, C. (1998) Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. Nat. Struct. Biol. 5, 476–48
Krause, K. H. and Michalak, M. (1997) Calreticulin. Cell 88, 439–443.
Maclennan, D. H., Campbell, K. P., and Reithmeier, R. A. F. (1983) Calsequestrin. Calcium and Cell Function 4, 151.
MacLennan, D. H. and Reithmeier, R. A. (1998) Ion tamers. Nat. Struct. Biol. 5, 409–411.
Rall, J. A. (1996) News Physiol. Sci. 11, 249–255.
Lytton, J. and MacLennan, D. H. (1992) Sarcoplasmic reticulum, in The Heart and Cardiovascular System. (Fozzard, H. A., Harber, E., Jennings, R. B., Katz, A. M., and Morgan, H. E., eds.), 2nd ed., Raven, New York, pp. 1203–1222.
Mitchell, R. D., Simmerman, H. K. B. and Jones, L. R. (1988) Ca2+binding effects on protein conformation and protein interactions of canine cardiac calsequestrin. J. Biol. Chem. 263, 1376–1381.
Guo, W. and Campbell, K. R (1995) Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum. J. Biol. Chem. 270, 9027–9030.
Inui, M., Saito, A., and Fleischer, S. (1987) Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle. J. Biol. Chem. 262, 1740–1747.
Ikemoto, N., Nagy, B., Bhatnagar, G. M., and Gergely, J. (1974) Studies on a metalbinding protein of the sarcoplasmic reticulum. J. Biol. Chem. 249, 2357–2365.
Ostwald, T. J. MacLennan, D. H., and Dorrington, K. J. (1974) Effects of cation binding on the conformation of calsequestrin and the high affinity calcium-binding protein of sarcoplasmic reticulum. J. Biol. Chem. 249, 5867–5871.
Aaron, B. M., Oikawa, K., Reithmeier, R. A., and Sykes B. D. (1984) Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. J. Biol. Chem. 259, 11,876–11,881.
He, Z., Dunker, A. K., Wesson, C. R., and Trumble, W. R. (1993) Ca(2+)-induced folding and aggregation of skeletal muscle sarcoplasmic reticulum calsequestrin. The involvement of the trifluoperazine-binding site. J. Biol. Chem. 268, 24,635–24,641.
Ikemoto, N., Bhatnagar, G. M. Nagy, B., and Gergely, J. (1972) Interaction of divalent cations with the 55,000-dalton protein component of the sarcoplasmic reticulum. Studies of fluorescence and circular dichroism. J. Biol. Chem. 247, 7835–7837.
Cozens, B. and Reithmeier, R. A. (1984) Size and shape of rabbit skeletal muscle calsequestrin. J. Biol. Chem. 259, 6248–6252.
Ohnishi, M. and Rethmeier, R. A. (1987) Fragmentation of rabbit skeletal muscle calsequestrin: spectral and ion binding properties of the carboxyl-terminal region. Biochemistry 26, 7458–7465.
Tanaka, M., Ozawa, T., Maurer, A. M., Cortese, J., and Fleischer, S. (1986) Apparent cooperativity of Ca2+binding associated with crystallization of Ca2+-binding protein from sarcoplasmic reticulum. Arch. Biochem. Biophys. 251, 369–378.
Franzini-Armstrong, C., Kenney, L. J., and Varriano-Marston, E. (1987) The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study. J. Cell Biol. 105, 49–56.
Saito, A., Seiler, S., Chu, A., and Fleischer, S. (1984) Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle. J. Cell Biol. 99, 875–885.
Maurer, A., Tanaka, M., Ozawa, T., and Fleischer, S. (1985) Purification and crystallization of the calcium binding protein of sarcoplasmic reticulum from skeletal muscle. Proc. Natl. Acad. Sci. USA 82, 4036–4040.
Maguire, P. B., Briggs, F. N., Lennon, N. J., and Ohlendieck, K. (1997) Oligomerization is an intrinsic property of calsequestrin in normal and transformed skeletal muscle. Biochem. Biophys. Res. Commun. 240, 721–727.
Ohgushi, M. and Wada, A. (1983) Molten-globule state: a compact form of globular proteins with mobile side-chains. FEBS Lett. 164, 21–24.
Dolgikh, D. A., Gilmanshin, R. I., Brazhnikov, E. V., Bychkova, V. E., Semisotnov, G. V., Venyaminov, S. Yu., and Ptitsyn, O. B. (1981) Alpha-Lactalbumin: compact state with fluctuating tertiary structure? FEBS Lett. 136, 311–315.
Ptisyn, O. B. (1995) Molten globule and protein folding. Adv. Protein Chem. 47, 83–229.
McPherson, A. (1990) Current approaches to macromolecular crystallization. Eur. J. Biochem. 189, 1–23.
Jancarik, J. and Kim, S.-H. (1991) Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Cryst. 24, 409–411.
Fliegel, L., Ohnishi, M., Carpenter, M. R., Khanna, V. K., Reithmeier, R. A. and MacLennan, D. H. (1987) Amino acid sequence of rabbit fast-twitch skeletal muscle calsequestrin deduced from cDNA and peptide sequencing. Proc. Natl. Acad. Sci. USA. 84, 1167–1171.
Scott, B. T., Simmerman, H. K., Collins, J. H., Nadal-Ginard, B., and Jones, L. R. (1988) Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning. J. Biol. Chem. 263, 8958–8964.
Freier R. K. (1976) Aqueous Solutions: Data for Inorganic and Organic Compounds, vol. 1. Walter de Gruyter, New York.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Humana Press Inc.
About this protocol
Cite this protocol
Kang, C., Trumble, W.R., Dunker, A.K. (2002). Crystallization and Structure-Function of Calsequestrin. In: Vogel, H.J. (eds) Calcium-Binding Protein Protocols. Methods in Molecular Biology™, vol 172. Humana Press. https://doi.org/10.1385/1-59259-183-3:281
Download citation
DOI: https://doi.org/10.1385/1-59259-183-3:281
Publisher Name: Humana Press
Print ISBN: 978-0-89603-688-8
Online ISBN: 978-1-59259-183-1
eBook Packages: Springer Protocols