2PHN
Crystal structure of an amide bond forming F420-gamma glutamyl ligase from Archaeoglobus fulgidus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-30 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97940 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 98.367, 98.367, 94.347 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.350 |
| R-factor | 0.16179 |
| Rwork | 0.160 |
| R-free | 0.18997 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2g9i |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.564 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.370 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.055 | 0.490 |
| Number of reflections | 99727 | |
| <I/σ(I)> | 22.3 | 4.69 |
| Completeness [%] | 98.7 | 97.9 |
| Redundancy | 8.2 | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 289 | 0.2 M Ammonium acetate, 0.1 M Sodium citrate, 25% PEG 5000 MME, 10 mM GDP, MnCl2, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
