3R07
Structural analysis of an archaeal lipoylation system. A bi-partite lipoate protein ligase and its E2 lipoyl domain from Thermoplasma acidophilum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 200 |
| Detector technology | CCD |
| Collection date | 2009-10-26 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 118.570, 118.570, 72.920 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 38.810 - 2.700 |
| R-factor | 0.2 |
| Rwork | 0.198 |
| R-free | 0.25400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ars |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.547 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 38.810 |
| High resolution limit [Å] | 2.700 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | 291 | 40% v/v MPD, 0.1M sodium acetate, 0.02M calcium chloride, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
