Abstract

The present work reports our succesfull experience concerning crystallization of four fish hemoglobins from three Brazilian species of Teleosts: Liposarcus anisitsi, Brycon cephalus and Piaractus mesopotamicus. The data shown here is part of a systematic functional and structural study of fish hemoglobins with the aim of better understanding the outstanding range of functional and structural properties exhibited by these proteins. We also present a reduced sparse-matrix method for crystallization of fish hemoglobins, which can reduce the amount of hemoglobin initially used in the crystallization experiments.

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