Crystallization and preliminary X-ray crystallographic analysis of rat calcineurin B homologous protein 1
| Autor: | Mamoru Sato, Kyouhei Arita, Youichi Naoe, Toshiyuki Shimizu, Hiroshi Kanazawa, Hiroshi Hashimoto |
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| Rok vydání: | 2005 |
| Předmět: |
Lipoproteins
Biophysics macromolecular substances Biochemistry Polyethylene Glycols law.invention Serine Bacterial Proteins X-Ray Diffraction Structural Biology law Calcium-binding protein Escherichia coli Genetics Animals Cloning Molecular Threonine Crystallization Protein kinase A Chemistry Effector Calcium-Binding Proteins Space group Condensed Matter Physics Rats Calcineurin Crystallography Crystallization Communications biological sciences Volatilization |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:612-613 |
| ISSN: | 1744-3091 |
| Popis: | Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding protein that plays a role in membrane trafficking and binds to multiple effector proteins, including Na+/H+ exchangers, serine/threonine protein kinase and calcineurin, potentially modulating their function. CHP1 has been crystallized at 277 K using polyethylene glycol as a precipitant. The crystal belongs to space group P2(1), with unit-cell parameters a = 55.5, b = 38.5, c = 90.0 A, beta = 90.7 degrees. A full set of diffraction data was collected to 2.2 A resolution at 100 K using the Photon Factory synchrotron-radiation source. |
| Databáze: | OpenAIRE |
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