Crystallization, preliminary X-ray analysis and molecular-replacement solution of the carboxy form of haemoglobin I from the fish Brycon cephalus.
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 A 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 (alphabeta) in the asymmetric unit. The structure was determined using standard molecular-replacement techniques.
Honda
R T
RT
Departamento de Física, Instituto de Biociências, Letras e Ci encias Exatas, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
Delatorre
P
P
Fadel
V
V
Canduri
F
F
Dellamano
M
M
de Azevedo
W F
WF
Bonilla-Rodriguez
G O
GO
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D005399:Fishes; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation
D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D000255:Adenosine Triphosphate; C026236:hemoglobin I, non-mammalian