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http://acervodigital.unesp.br/handle/11449/39487- Título:
- Crystallization, preliminary X-ray analysis and molecular-replacement solution of the carboxy form of haemoglobin I from the fish Brycon cephalus
- Universidade Estadual Paulista (UNESP)
- Faciba FEB
- Ctr Univ Votuporanga
- 0907-4449
- Haemoglobin, the 'honorary enzyme' [Brunori (1999), Trends Biochem. Sci. 24, 158-161], constitutes a prime prototype for allosteric models. Here, the crystallization and preliminary X-ray analysis of haemoglobin I from the South American fish Brycon cephalus are reported. X-ray diffraction data have been collected to 2.5 Angstrom resolution using synchrotron radiation (LNLS). Crystals were determined to belong to the space group P6(1)22 and preliminary structural analysis revealed the presence of one dimer (alpha beta) in the asymmetric unit. The structure was determined using standard molecular-replacement techniques.
- 1-Dez-2000
- Acta Crystallographica Section D-biological Crystallography. Copenhagen: Munksgaard Int Publ Ltd, v. 56, p. 1685-1687, 2000.
- 1685-1687
- Munksgaard Int Publ Ltd
- http://dx.doi.org/10.1107/S0907444900015262
- Acesso restrito
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- http://repositorio.unesp.br/handle/11449/39487
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