Abstract
The fungal immunomodulatory protein from the edible golden needle mushroom (Flammulina velutipes), designated Fve, is a single polypeptide consisting of 114 amino-acid residues. It is believed to trigger the mitogenic proliferation of T lymphocytes and Th1 cytokine production. Here, it is demonstrated that Fve forms a homodimer in nature. In order to understand the relationship between its structure and function, Fve was crystallized using the hanging-drop method; the protein formed well diffracting crystals within 3-5 d in 2.5% PEG 400, 2.0 M ammonium sulfate and 0.1 M Tris base buffer pH 8.5. The space group of the Fve crystals is either P43212 or P412 12, with unit-cell parameters a =- b = 96.92, c = 61.42 Å. The crystal contains two molecules per asymmetric unit and diffracts to 1.4 Å resolution when exposed to synchrotron radiation.
| Original language | English |
|---|---|
| Pages (from-to) | 1487-1489 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section D: Structural Biology |
| Volume | 59 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 1 Aug 2003 |
| Externally published | Yes |
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