26AO
E. coli peptidyl-prolyl cis-trans isomerase, mutant F4/F5Phe
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX3 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2026-02-13 |
| Detector | DECTRIS EIGER2 XE 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 1 |
| Unit cell lengths | 34.914, 39.199, 61.618 |
| Unit cell angles | 78.04, 79.29, 67.01 |
Refinement procedure
| Resolution | 31.920 - 1.150 |
| R-factor | 0.1987 |
| Rwork | 0.197 |
| R-free | 0.22600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.136 |
| Data reduction software | xia2 |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.680 | 1.170 |
| High resolution limit [Å] | 1.150 | 1.150 |
| Rmerge | 0.077 | 1.040 |
| Rmeas | 0.094 | 1.255 |
| Rpim | 0.053 | 0.689 |
| Total number of observations | 346528 | 15038 |
| Number of reflections | 98202 | 4606 |
| <I/σ(I)> | 7.7 | 1 |
| Completeness [%] | 94.6 | |
| Redundancy | 3.5 | 3.3 |
| CC(1/2) | 0.962 | 0.470 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | 35% PEG 3350, 0.2M Sodium acetate trihydrate, 0.1M TRIS hydrochloride pH 8.0 |
