Crystallization, preliminary X-ray analysis and molecular-replacement solution of the carboxy form of haemoglobin I from the fish Brycon cephalus
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
01/12/2000
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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 |