2G9I
Crystal structure of homolog of F420-0:gamma-Glutamyl Ligase from Archaeoglobus fulgidus Reveals a Novel Fold.
Experimental procedure
Experimental method | SAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-06-20 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9795 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 100.386, 100.386, 92.960 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.500 |
R-factor | 0.19351 |
Rwork | 0.190 |
R-free | 0.25484 |
Structure solution method | SAD |
RMSD bond length | 0.020 |
RMSD bond angle | 1.826 |
Data scaling software | HKL-2000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.109 | |
Number of reflections | 16992 | |
<I/σ(I)> | 40.3 | 5.1 |
Completeness [%] | 100.0 | 100 |
Redundancy | 30.4 | 24.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 291 | 30% PEG 2K MME, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K |