Abstract
A putative aspartate aminotransferase from the hyperthermophilic archaeon Methanococcus jannaschii encoded by the Mj0684 gene has been overexpressed in Escherichia coli and crystallized at 296 K using the sitting-drop vapour-diffusion method. The crystals belong to space group P41212 (or P43212), with unit-cell parameters a = b = 111.87, c = 60.86 Å. They diffract to 2.2 Å resolution using Cu Kα X-rays. The asymmetric unit contains a single subunit of the recombinant Mj0684 gene product, giving a corresponding VM of 2.25 Å3 Da-1 and a solvent content of 45.3% by volume. An X-ray diffraction data set has been collected to 2.2 Å at 295 K.
| Original language | English |
|---|---|
| Pages (from-to) | 563-565 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section D: Structural Biology |
| Volume | 59 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1 Mar 2003 |