Description:
<jats:p>The <jats:italic>metC</jats:italic> gene coding for cystathionine β‐lyase of <jats:italic>Escherichia coli</jats:italic> has been cloned and used to construct an overproducing <jats:italic>E. coli</jats:italic> strain. An efficient purification scheme has been developed and the purified enzyme has been crystallized by the hanging drop vapour diffusion method using either ammonium sulfate or polyethyleneglycol 400 as precipitating agent. The crystals belong to the orthorombic space group C222<jats:sub>1</jats:sub>. Their unit cell parameters are <jats:inline-graphic xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="graphic/feb20014579395014993-math-si1.gif" xlink:title="urn:x-wiley:00145793:media:feb20014579395014993:feb20014579395014993-math-si1" />. Consideration of the possible values of <jats:italic>V</jats:italic>
<jats:sub>M</jats:sub> accounts for the presence of one dimer per asymmetric unit. The crystals are suitable for X‐ray analysis and a complete native date set to 1.83 Å resolution has been collected using synchrotron radiation.</jats:p>