Expression, crystallization and preliminary X-ray crystallographic analysis of aldehyde dehydrogenase (ALDH) from Bacillus cereus

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2013-05, Vol.69 (5), p.528-531
• Main Authors: Ngo, Ho-Phuong-Thuy, Hong, Seung-Hye, Oh, Deok-Kun, Kang, Lin-Woo
• Format: Article
• Language: English
• Subjects: Aldehyde Dehydrogenase - chemistry; Aldehyde Dehydrogenase - genetics; Aldehyde Dehydrogenase - isolation & purification; aldehyde dehydrogenases; Aldehydes; ALDH; Asymmetry; Bacillus cereus; Bacillus cereus - enzymology; Crystallization; Crystallization Communications; Crystallography; Crystallography, X-Ray; Dehydrogenase; Diffraction; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Genes; Proteins
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S1744309113007288

Aldehyde dehydrogenase (ALDH) catalyses the oxidation of aldehydes using NAD(P)+ as a cofactor. Most aldehydes are toxic at low levels. ALDHs are used to regulate metabolic intermediate aldehydes. The aldh gene from Bacillus cereus was cloned and the ALDH protein was expressed, purified and crystallized. A crystal of the ALDH protein diffracted to 2.6 Å resolution and belonged to the monoclinic space group P21, with unit‐cell parameters a = 83.5, b = 93.3, c = 145.5 Å, β = 98.05°. Four protomers were present in the asymmetric unit, with a corresponding VM of 2.55 Å3 Da−1 and a solvent content of 51.8%.