Abstract
The NAD-dependent malonate-semialdehyde dehydrogenase KES23460 from Pseudomonas sp. strain AAC makes up half of a bicistronic operon responsible for β-alanine catabolism to produce acetyl-CoA. The KES23460 protein has been heterologously expressed, purified and used to generate crystals suitable for X-ray diffraction studies. The crystals belonged to space group P212121 and diffracted X-rays to beyond 3 Å resolution using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4zz7 as the search model.The crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC has been determined to a nominal resolution of 2.95 Å.
| Original language | English |
|---|---|
| Pages (from-to) | 24-28 |
| Number of pages | 5 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 73 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1 Jan 2017 |
| Externally published | Yes |
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