4DZ2
Crystal structure of a Peptidyl-prolyl cis-trans isomerase with surface mutation R92G from Burkholderia pseudomallei complexed with FK506
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-10-04 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 106.440, 49.050, 66.640 |
| Unit cell angles | 90.00, 123.05, 90.00 |
Refinement procedure
| Resolution | 44.610 - 2.000 |
| R-factor | 0.22 |
| Rwork | 0.219 |
| R-free | 0.24700 |
| Structure solution method | MR |
| Starting model (for MR) | 3vaw |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.473 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 44.610 | 2.050 | |
| High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
| Rmerge | 0.047 | 0.034 | 0.131 |
| Number of reflections | 19250 | 234 | 1392 |
| <I/σ(I)> | 26.88 | 48.6 | 9.1 |
| Completeness [%] | 97.5 | 95.1 | 96.6 |
| Redundancy | 6.44 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 290 | Internal tracking number 224744. JCSG well D10. 0.1M Cacodylate pH 6.5, 200mM Calcium Acetate, 30.0% w/v PEG400, 20% Ethylene Glycol Cryo. BupsA.00130.a.D239 PD00214 21.8mg/ml, vapor diffusion, sitting drop, temperature 290K, VAPOR DIFFUSION, SITTING DROP |
