Beschreibung:
<jats:p>Tyrosine aminotransferase from <jats:italic>Trypanosoma cruzi</jats:italic> has been crystallized from PEG 4000 at pH 6.8. The crystals belong to the monoclinic space group <jats:italic>P</jats:italic>2<jats:sub>1</jats:sub> and have lattice constants of <jats:italic>a</jats:italic> = 59.1, <jats:italic>b</jats:italic> = 103.0, <jats:italic>c</jats:italic> = 77.8 Å, β = 113.1° for a data set measured at 138 K. The presence of a non-crystallographic twofold axis together with a Matthews parameter <jats:italic>V<jats:sub>m</jats:sub>
</jats:italic> of 2.5 Å<jats:sup>3</jats:sup> Da<jats:sup>−1</jats:sup> indicates that the asymmetric unit contains one dimeric molecule. The crystals diffract to at least 2.7 Å and are stable in the X-ray beam in a shock-frozen state. Native data sets have been collected at temperatures of 285 and 138 K using a Siemens X1000 detector on a rotating-anode generator.</jats:p>