3K2C
Crystal structure of peptidyl-prolyl cis-trans isomerase from Encephalitozoon cuniculi at 1.9 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-09-18 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97351 |
| Spacegroup name | P 1 |
| Unit cell lengths | 38.810, 73.860, 63.590 |
| Unit cell angles | 90.01, 79.10, 90.02 |
Refinement procedure
| Resolution | 40.000 - 1.950 |
| R-factor | 0.166 |
| Rwork | 0.163 |
| R-free | 0.21600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2biu |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.515 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.000 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.052 | 0.276 |
| Number of reflections | 47719 | |
| <I/σ(I)> | 11.91 | 3 |
| Completeness [%] | 94.4 | 94.7 |
| Redundancy | 2 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 290 | HAMPTON RESEARCH CRYSTAL SCREEN CONDITION B5: 200mM Li sulfate, 100mM Tris-HCl pH 8.5, 30% PEG 4000; Protein at 49.8 mg/mL, VAPOR DIFFUSION, SITTING DROP, temperature 290.0K |
