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 |
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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 |