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Purification, crystallization and preliminary crystallographic analysis of the CBS‐domain pair of cyclin M2 (CNNM2)

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This work describes the purification and preliminary crystallographic analysis of the CBS‐domain pair of the murine CNNM2 magnesium transporter (formerly known as ancient domain protein 2; ACDP2), which consists of a pair of cystathionine β‐synthase (CBS) motifs and has 100% sequence identity to its human homologue. CNNM proteins represent the least‐studied members of the eight different types of magnesium transporters identified to date in mammals. In humans, the CNNM family is encoded by four genes: CNNM1–4. CNNM1 acts as a cytosolic copper chaperone, whereas CNNM2 and CNNM4 have been associated with magnesium handling. Interestingly, mutations in the CNNM2 gene cause familial dominant hypomagnesaemia (MIM:607803), a rare human disorder characterized by renal and intestinal magnesium (Mg2+) wasting, which may lead to symptoms of Mg2+ depletion such as tetany, seizures and cardiac arrhythmias. This manuscript describes the preliminary crystallographic analysis of two different crystal habits of a truncated form of the protein containing its regulatory CBS‐domain pair, which has been reported to host the pathological mutation T568I in humans. The crystals belonged to space groups P21212 and I222 (or I212121) and diffracted X‐rays to 2.0 and 3.6 Å resolution, respectively, using synchrotron radiation.
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Document Type: Research Article

Publication date: 2012-10-01

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