Abstract
Bothropstoxin I (BthTX-I), a non-catalytic and myotoxic Lys49-PLA2 from Bothrops jararacussu venom, has been crystallized alone and complexed with -tocopherol inhibitor. These crystals have been shown to diffract X-rays be- tween 2.17 and 1.83 A resolution. The BthTX-I/ -tocopherol complex crystals are not isomorphous with those of the na- tive protein. This suggests the inhibitor binding has lead to changes in the quaternary structure and a different conforma- tion may have been obtained.
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