6XD8
Crystal Structure of Peptidylprolyl Isomerase (PrsA) Fragment from Bacillus anthracis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2020-02-14 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 48.889, 107.344, 31.698 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.310 - 1.520 |
| R-factor | 0.1722 |
| Rwork | 0.170 |
| R-free | 0.22190 |
| Structure solution method | SAD |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.285 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.550 |
| High resolution limit [Å] | 1.520 | 1.520 |
| Rmerge | 0.061 | 0.723 |
| Rmeas | 0.066 | 0.780 |
| Rpim | 0.025 | 0.289 |
| Number of reflections | 26434 | 1272 |
| <I/σ(I)> | 28.5 | 2.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.1 | 7.2 |
| CC(1/2) | 0.817 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 292 | Protein: 7.8 mg/ml, 0.01M Tris pH 8.3; Screen: Classics II (H11), 0.1M Potassium thiocyanate, 30% (w/v) PEG 2000 MME |
