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This work describes the purification and preliminary crystallographic analysis of the CBS-domain pair of the murine CNNM2 magnesium transporter, which consists of a pair of cystathionine β-synthase (CBS) motifs and has 100% sequence identity to its human homologue.

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This article describes the crystallization and preliminary crystallographic analysis of a protein construct (hCBS516–525) that contains the full-length cystathionine β-synthase from Homo sapiens (hCBS) and just lacks amino-acid residues 516–525.

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This manuscript describes the crystallization of the full-length enzyme cystathionine β-synthase (CBS) from Apis mellifera, which maintains 46% sequence identity with the human homolog. Mutations in CBS cause hereditary homocystinuria in humans.
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