2F3O
Crystal Structure of a glycyl radical enzyme from Archaeoglobus fulgidus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-02-21 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.00 |
Spacegroup name | C 2 2 2 |
Unit cell lengths | 167.030, 174.170, 162.460 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.690 - 2.900 |
R-factor | 0.202 |
Rwork | 0.199 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1r9d |
RMSD bond length | 0.011 |
RMSD bond angle | 1.545 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.087 | 0.449 |
Number of reflections | 52531 | 4896 |
<I/σ(I)> | 20.61 | 5.34 |
Completeness [%] | 98.6 | 97.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 16 % PEG8000, 8 % isopropanol, 80 mM Hepes pH 7.5, 160 mM ammonium sulphate, 1 mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K |