Abstract
In order to analyze the alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus, the N-terminal fragment lacking the dimerization domain and the C-terminal dimerization-domain fragment were each overexpressed in Escherichia coli, purified and crystallized. A 3.7 Å resolution data set was collected for the N-terminal fragment. The crystal belongs to the tetragonal space group P41 or P43, with unit-cell parameters a = b = 101.15, c = 124.24 Å. For the C-terminal fragment, a SeMet MAD data set was collected to 3.2 Å resolution. The crystal belongs to the orthorhombic space group P2221, with unit-cell parameters a = 124.15, b = 131.91, c = 138.68 Å.
Original language | English (US) |
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Pages (from-to) | 224-228 |
Number of pages | 5 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 63 |
Issue number | 3 |
DOIs | |
State | Published - Feb 13 2007 |
Externally published | Yes |
Keywords
- AlaRS
- Alanine
- Archaeoglobus fulgidus
- Dimerization
- Editing
- tRNa
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics