5V7Y
Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 4.2.2 |
| Synchrotron site | ALS |
| Beamline | 4.2.2 |
| Temperature [K] | 100 |
| Detector technology | CMOS |
| Collection date | 2016-04-19 |
| Detector | RDI CMOS_8M |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.238, 106.826, 81.056 |
| Unit cell angles | 90.00, 103.65, 90.00 |
Refinement procedure
| Resolution | 63.397 - 2.050 |
| R-factor | 0.1635 |
| Rwork | 0.161 |
| R-free | 0.20860 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5iax |
| RMSD bond length | 0.012 |
| RMSD bond angle | 0.876 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.28) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 63.400 | 63.400 | 2.110 |
| High resolution limit [Å] | 2.050 | 8.940 | 2.050 |
| Rmerge | 0.092 | 0.024 | 0.475 |
| Rmeas | 0.108 | 0.028 | 0.560 |
| Rpim | 0.057 | 0.014 | 0.294 |
| Number of reflections | 51889 | ||
| <I/σ(I)> | 13.3 | ||
| Completeness [%] | 99.5 | 98.1 | 99.9 |
| Redundancy | 3.6 | 3.6 | 3.6 |
| CC(1/2) | 0.996 | 0.999 | 0.813 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 0.1 M imidazole pH 8.0, 5% PEG 4000, 15% MPD |






