6B8D
1.78 Angstrom Resolution Crystal Structure of N-terminal Fragment (residues 1-405) of Elongation Factor G from Haemophilus influenzae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-08-08 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 84.823, 88.487, 130.279 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.800 - 1.780 |
| R-factor | 0.17457 |
| Rwork | 0.173 |
| R-free | 0.21366 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5tv2 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.368 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MoRDa |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.810 |
| High resolution limit [Å] | 1.780 | 1.780 |
| Rmerge | 0.043 | 0.797 |
| Rpim | 0.018 | 0.325 |
| Number of reflections | 47575 | 2388 |
| <I/σ(I)> | 38.4 | 2.6 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 6.9 | 6.9 |
| CC(1/2) | 0.832 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 295 | 11.0 mg/mL protein in 0.5 M sodium chloride, 0.01 M Tris-HCl, pH 8.3 against screen: Classics II (F6), 0.2 M ammonium sulfate, 0.1 M Bis-Tris, pH 5.5, 25% w/v PEG3350 |






