7RFD
E. coli peptidyl-prolyl cis-trans isomerase, mutant Phe4Ala Phe27CF3-Phe/Phe98CF3-Phe
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-06-13 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 61 |
| Unit cell lengths | 34.891, 34.891, 210.047 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.010 - 1.350 |
| R-factor | 0.1232 |
| Rwork | 0.122 |
| R-free | 0.14900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7n3j |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.191 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.7) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 35.010 | 35.010 | 1.370 |
| High resolution limit [Å] | 1.350 | 7.390 | 1.350 |
| Rmerge | 0.249 | 0.055 | 3.832 |
| Rmeas | 0.257 | 0.057 | 4.041 |
| Rpim | 0.060 | 0.013 | 1.253 |
| Total number of observations | 545282 | 4122 | 14540 |
| Number of reflections | 31687 | 216 | 1539 |
| <I/σ(I)> | 13.1 | 43.2 | 1.3 |
| Completeness [%] | 100.0 | 99.9 | 100 |
| Redundancy | 17.2 | 19.1 | 9.4 |
| CC(1/2) | 0.998 | 0.998 | 0.426 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 40% PEG 3350, 0.1M Tris-HCl (pH 8.0), 0.2M Sodium Acetate |
