Please use this identifier to cite or link to this item:
- Crystallization, preliminary X-ray analysis and molecular-replacement solution of haemoglobin-II from the fish matrinxa (Brycon cephalus)
- Universidade Estadual Paulista (UNESP)
- Haemoglobins constitute a set of proteins with interesting structural and functional properties, especially when the two large animal groups reptiles and fishes are focused on. Here, the crystallization and preliminary X-ray analysis of haemoglobin-II from the South American fish matrinxa (Brycon cephalus) is reported. X-ray diffraction data have been collected to 3.0 Angstrom resolution using synchrotron radiation (LNLS). Crystals were determined to belong to space group P2(1) and preliminary structural analysis revealed the presence of two tetramers in the asymmetric unit. The structure was determined using the standard molecular-replacement technique.
- Acta Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 59, p. 752-754, 2003.
- Blackwell Munksgaard
- Acesso restrito
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.