Crystallization of β-galactosidase does not reduce the range of activity of individual molecules

Biochemistry

Volumn 42, Issue 6, 2003, Pages 1707-1710

  Shoemaker, Glen K ^a   Juers, Douglas H ^b   Coombs, Jennifer M L ^a   Matthews, Brian W ^b   Craig, Douglas B ^a  

^a UNIVERSITY OF WINNIPEG   (Canada)

^b UNIVERSITY OF OREGON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLIZATION; CRYSTALS; ELECTROPHORESIS; ENZYMES; MOLECULES;

ENZYME PREPARATION;

BIOCHEMISTRY;

BETA GALACTOSIDASE;

ARTICLE; CAPILLARY ELECTROPHORESIS; CHEMICAL REACTION; CRYSTAL; CRYSTALLIZATION; ENZYME ACTIVITY; ENZYME ISOLATION; ENZYME PURIFICATION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

BETA-GALACTOSIDASE; CRYSTALLIZATION; ELECTROPHORESIS, CAPILLARY; ENZYME ACTIVATION; ESCHERICHIA COLI PROTEINS; FLUORESCENT DYES; GALACTOSIDES; OXAZINES; SUBSTRATE SPECIFICITY;

EID: 12244291015     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0204138     Document Type: Article

References (13)

1. Xue, Q., and Yeung, E. S. (1995) Differences in the Chemical Reactivity of Individual Molecules of an Enzyme, Nature 373, 681-683.
2. Craig, D. B., and Dovichi, N. J. (1998) E. coli β-galactosidase is Heterogeneous with Respect to the Activity of Individual Molecules, Can. J. Chem. 76, 623-626.
3. Craig, D. B., Arriaga, E. A., Wong, J. C. Y., Lu, H., and Dovichi, N. J. (1996) Studies on Single Alkaline Phosphatase Molecules: Reaction Rate and Activation Energy of a Reaction Catalyzed by a Single Molecule and the Effect of Thermal Denaturation - The Death of an Enzyme, J. Am. Chem. Soc. 118, 5245-5253.
4. Tan, W., and Yeung, E. S. (1997) Monitoring the Reactions of Single Enzyme Molecules and Single Metal Ions, Anal. Chem. 69, 4242-4248.
5. Edman, L., Foldes-Papp, Z., Wennmalm, S., and Rigler, R. (1999) The Fluctuating Enzyme: A Single Molecule Approach, Chem. Phys. 247, 11-22.
6. Lu, H. P., Sun, L., and Xie, X. S. (1998) Single-Molecule Enzymatic Dynamics, Science 282, 1877-1882.
7. Juers, D. H., Jacobson, R. H., Wigley, D., Zhang, X.-J., Huber. R. E., Tronrud, D. E., and Matthews, B. W. (2000) High-Resolution Refinement of β-galactosidase in a New Crystal Form Reveals Multiple Metal-binding Sites and Provides a Structural Basis for a-Complementation, Protein Sci. 9, 1685-1699.
8. Craig, D., Arriaga, E. A., Banks, P., Zhang, Y., Renborg, A., Palcic, M. M., and Dovichi, N. J. (1995) Fluorescence-based Enzymatic Assay by Capillary Electrophoresis Laser-induced Fluorescence Detection for the Determination of a Few β-Galactosidase Molecules, Anal. Biochem. 226, 147-153.
9. Snedecor, G. W., and Cochran, W. G. (1980) Statistical methods, 7th ed., Iowa State University Press, Ames, IA.
10. Chen, D. Y., and Dovichi, N. J. (1994) Yoctomolar Detection Limit by Laser-induced Fluorescence in Capillary Electrophoresis, J. Chromatogr. B 657, 265-269.
11. Craig, D. B., Hall, T., and Goltz, D. M. (2000) E. coli β-Galactosidase is Heterogeneous with Respect to a Requirement for Magnesium, BioMetals 13, 223-229.
12. Alpers, D. H., Steers, E., Jr., Shifrin, S., and Tomkins, G. (1968) Isozymes of the Lactose Operon of Escherichia coli, Ann. N.Y. Acad. Sci. 151, 545-555.
13. Appel, S. H., Alpers, D. H., and Tomkins, G. M. (1965) Multiple Molecular Forms of β-Galactosidase, J. Mol. Biol. 11, 12-22.