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Crystallographic study of wild-type carbonic anhydrase αCA1 from<i>Chlamydomonas reinhardtii</i>
Description
<jats:p>Carbonic anhydrases (CAs) are ubiquitously distributed and are grouped into three structurally independent classes (αCA, βCA and γCA). Most αCA enzymes are monomeric, but αCA1 from<jats:italic>Chlamydomonas reinhardtii</jats:italic>is a dimer that is uniquely stabilized by disulfide bonds. In addition, during maturation an internal peptide of 35 residues is removed and three asparagine residues are glycosylated. In order to obtain insight into the effects of these structural features on CA function, wild-type<jats:italic>C. reinhardtii</jats:italic>αCA1 has been crystallized in space group<jats:italic>P</jats:italic>6<jats:sub>5</jats:sub>, with unit-cell parameters<jats:italic>a</jats:italic>=<jats:italic>b</jats:italic>= 134.3,<jats:italic>c</jats:italic> = 120.2 Å. The crystal diffracted to 1.88 Å resolution and a preliminary solution of its crystal structure has been obtained by the MAD method.</jats:p>
Journal
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- Acta Crystallographica Section F Structural Biology and Crystallization Communications
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Acta Crystallographica Section F Structural Biology and Crystallization Communications 66 1082-1085, 2010-08-28
International Union of Crystallography (IUCr)
