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<jats:title>A biotech tour de force</jats:title> <jats:p> RuBisCo, the key enzyme of photosynthesis, is a complex of eight large and eight small subunits. It mediates the fixation of atmospheric CO <jats:sub>2</jats:sub> in the Calvin-Benson-Bassham cycle. In addition to being enzymatically inefficient, RuBisCo has a problem with distinguishing between CO <jats:sub>2</jats:sub> and O <jats:sub>2</jats:sub> . The fixation of O <jats:sub>2</jats:sub> results in the energetically wasteful reaction of photorespiration. Thus, there is a strong incentive to improve RuBisCo's catalytic properties by engineering. However, for decades, it has been impossible to express the enzyme from plants in an easily manipulatable bacterial host. Aigner <jats:italic>et al.</jats:italic> succeeded in functionally expressing plant RuBisCo in <jats:italic>Escherichia coli</jats:italic> (see the Perspective by Yeates and Wheatley). This should allow for the systematic mutational analysis of RuBisCo and selection of favorable variants for improved crop yields. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6368" page="1272" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aap9221">1272</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6368" page="1253" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aar3107">1253</jats:related-article> </jats:p>