Cadmium-induced crystallization of proteins: II. Crystallization of the Salmonella typhimurium histidine-binding protein in complex with L-histidine, L-arginine, or L-lysine
| Autor: | Giovanna Ferro-Luzzi Ames, David I. Kreimer, S. Trakhanov, Bernhard Rupp, Sean Parkin |
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| Rok vydání: | 1998 |
| Předmět: |
inorganic chemicals
Salmonella typhimurium Lysine chemistry.chemical_element Arginine Biochemistry law.invention Divalent Protein structure law Histidine Crystallization Molecular Biology chemistry.chemical_classification Cadmium Ligand (biochemistry) Crystallography chemistry Periplasmic Binding Proteins Protein crystallization Carrier Proteins Research Article |
| Zdroj: | Protein science : a publication of the Protein Society. 7(3) |
| ISSN: | 0961-8368 |
| Popis: | To further investigate favorable effects of divalent cations on the formation of protein crystals, three complexes of Salmonella typhimurium histidine-binding protein were crystallized with varying concentrations of cadmium salts. For each of the three histidine-binding protein complexes, cadmium cations were found to promote or improve crystallization. The optimal cadmium concentration is ligand specific and falls within a narrow concentration range. In each case, crystals grown in the presence of cadmium diffract to better than 2.0 angstroms resolution and belong to the orthorhombic space group P2(1)2(1)2(1). From our results and from the analysis of cadmium sites in well-refined protein structures, we propose that cadmium addition provides a generally useful technique to modify crystal morphology and to improve diffraction quality. |
| Databáze: | OpenAIRE |
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