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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/39487
Title: 
Crystallization, preliminary X-ray analysis and molecular-replacement solution of the carboxy form of haemoglobin I from the fish Brycon cephalus
Author(s): 
Institution: 
  • Universidade Estadual Paulista (UNESP)
  • Faciba FEB
  • Ctr Univ Votuporanga
ISSN: 
0907-4449
Abstract: 
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.
Issue Date: 
1-Dec-2000
Citation: 
Acta Crystallographica Section D-biological Crystallography. Copenhagen: Munksgaard Int Publ Ltd, v. 56, p. 1685-1687, 2000.
Time Duration: 
1685-1687
Publisher: 
Munksgaard Int Publ Ltd
Source: 
http://dx.doi.org/10.1107/S0907444900015262
URI: 
Access Rights: 
Acesso restrito
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/39487
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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