Crystallization, preliminary X-ray analysis and molecular-replacement solution of the carboxy form of haemoglobin I from the fish Brycon cephalus


Autoria(s): Honda, R. T.; Delatorre, P.; Fadel, V; Canduri, F.; Dellamano, M.; de Azevedo, W. F.; Bonilla-Rodriguez, G. O.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/12/2000

Resumo

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.

Formato

1685-1687

Identificador

http://dx.doi.org/10.1107/S0907444900015262

Acta Crystallographica Section D-biological Crystallography. Copenhagen: Munksgaard Int Publ Ltd, v. 56, p. 1685-1687, 2000.

0907-4449

http://hdl.handle.net/11449/39487

10.1107/S0907444900015262

WOS:000165509100030

WOS000165509100030.pdf

Idioma(s)

eng

Publicador

Munksgaard Int Publ Ltd

Relação

Acta Crystallographica Section D: Biological Crystallography

Direitos

closedAccess

Tipo

info:eu-repo/semantics/article