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Updated: Jul 2, 2026
Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
Published on: May 10, 2014
Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine beta-synthase
Byung Cheon Jeong1, Kyoung Shin Yoo, Kwang Wook Jung
1School of Life Sciences and Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-701, Republic of Korea.
Abstract:
Cystathione beta-synthase domain-containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three-dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as a precipitant. The crystals diffracted to 2.4 A resolution using synchrotron radiation and belonged to the trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 56.360, c = 82.596 A, alpha = beta = 90, gamma = 120 degrees . The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%.
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