Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 69, Part 5 (May 2013)

crystallization communications

Acta Cryst. (2013). F69, 528-531    [ doi:10.1107/S1744309113007288 ]

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

H.-P.-T. Ngo, S.-H. Hong, D.-K. Oh and L.-W. Kang

Abstract: 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, [beta] = 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%.

Keywords: aldehyde dehydrogenases; ALDH; Bacillus cereus.

pdfdisplay filedownload file

Portable Document Format (PDF) file
[ doi:10.1107/S1744309113007288/nj5148sup1.pdf ]
Supplementary Table containing protein sequence.


To open or display or play some files, you may need to set your browser up to use the appropriate software. See the full list of file types for an explanation of the different file types and their related mime types and, where available links to sites from where the appropriate software may be obtained.

The download button will force most browsers to prompt for a file name to store the data on your hard disk.

Where possible, images are represented by thumbnails.

 bibliographic record in  format

  Find reference:   Volume   Page   
  Search:     From   to      Advanced search

Copyright © International Union of Crystallography
IUCr Webmaster