Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis
Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis(201 visite) Merlino A, Russo Krauss I, Albino A, Pica A, Vergara A, Masullo M, De Vendittis E, Sica F
Parole chiave: Crystal Quality, Glutathione Synthetase, Psychrophile, Without-Oil Microbatch, X-Ray Crystallography, Glutathione Synthase, Article, Concentration (parameters), Controlled Study, Crystal Structure, Enzyme Purification, Escherichia Coli, Evaporation, Process Optimization, Protein Expression, Pseudoalteromonas, Pseudoalteromonas Haloplanktis, Psychrophilic Bacterium, Quality Control, Structure Analysis, Validation Process, X Ray Diffraction,
Affiliazioni:
*** IBB - CNR *** Dipartimento di Chimica Paolo Corradini, Università di Napoli Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cinthia, Naples I-80126, Italy Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, Naples I-80134, Italy Dipartimento di Biochimica e Biotecnologie Mediche, Università di Napoli Federico II, Via Pansini 5, Naples I-80131, Italy Dipartimento di Studi delle Istituzioni e dei Sistemi Territoriali, Università di Napoli Parthenope, Via Medina 40, Naples I-80133, Italy
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Pallardo, F. V., Markovic, J., Garcia, J. L., Vina, J., Role of nuclear glutathione as a key regulator of cell proliferation (2009) Mol. Asp. Med, 30, pp. 77-85
Mooz, E. D., Meister, A., Tripeptide (glutathione) synthetase: Purification, properties and mechanism of action (1967) Biochemistry, 6, pp. 1722-1734
Gali, R. R., Board, P. G., Sequencing and expression of a cDNA for human glutathione synthetase (1995) Biochem. J, 310, pp. 353-358
Huang, C. S., He, W., Meister, A., Anderson, M. E., Amino acid sequence of rat kidney glutathione synthetase (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 1232-1236
Chayen, N. E., Shaw Stewart, P. D., Maeder, D. L., Blow, D. M., An automated system for micro-batch protein crystallization and screening (1990) J. Appl. Cryst, 23, pp. 297-302
Chayen, N. E., Recent advances in methodology for the crystallization of biological macromolecules (1999) J. Cryst. Growth, 199, pp. 649-655
Martins, P. M., Pessoa, J., Sarkany, Z., Rocha, F., Damas, A. M., Rationalizing protein crystallization Screenings through water equilibration theory and protein solubility data (2008) Cryst. Growth Des, 8, pp. 4233-4243
Matthews, B. W., Solvent content of protein crystals (1968) J. Mol. Biol, 33, pp. 491-497
Weiss, M. S., Global indicators of X-ray data quality (2001) J. Appl. Crystallogr, 34, pp. 130-135
Storoni, L. C., McCoy, A. J., Read, R. J., Likelihood-enhanced fast rotation functions (2004) Acta Crystallogr. D Biol. Crystallogr, 60, pp. 432-438
Glutathione synthetases catalyze the ATP-dependent synthesis of glutathione from L-gamma-glutamyl-L-cysteine and glycine. Although these enzymes have been sequenced and characterized from a variety of biological sources, their exact catalytic mechanism is not fully understood and nothing is known about their adaptation at extremophilic environments. Glutathione synthetase from the Antarctic eubacterium Pseudoalteromonas haloplanktis (PhGshB) has been expressed, purified and successfully crystallized. An overall improvement of the crystal quality has been obtained by adapting the crystal growth conditions found with vapor diffusion experiments to the without-oil microbatch method. The best crystals of PhGshB diffract to 2.34 angstrom resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 83.28 angstrom, b = 119.88 angstrom, c = 159.82 angstrom. Refinement of the model, obtained using phases derived from the structure of the same enzyme from Escherichia coli by molecular replacement, is in progress. The structural determination will provide the first structural characterization of a psychrophilic glutathione synthetase reported to date.
50 Records (49 escludendo Abstract e Conferenze). Impact factor totale: 189.634 (185.446 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 203.27 (196.107 escludendo Abstract e Conferenze).
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