Abstract
Glycine decarboxylase or P-protein is a major enzyme involved in the C1 metabolism of all organisms and in the photorespiratory pathway of plants and cyanobacteria. The protein from Synechocystis sp. PCC 6803 is a homodimer with a mass of 215 kDa. Recombinant glycine decarboxylase was expressed in Escherichia coli and purified with metal affinity-, ion exchange- and gel filtration chromatography. Crystals of P-protein that diffracted to a resolution of 2.1 Å were obtained using the hanging drop vapour diffusion method at 291 K. X-ray diffraction data were collected from cryo-cooled crystals using synchrotron radiation. The crystals belong to space group P212121 with unit cell parameters a = 96.30 Å, b = 135.81 Å, and c = 179.08 Å
| Original language | English |
|---|---|
| Pages (from-to) | 187-191 |
| Number of pages | 5 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 66 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2010 |
Keywords
- glycine decarboxylase
- P-protein
- crystallization
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