7L6Y
Crystal Structure of the Peptidyl-Prolyl Cis-Trans Isomerase (PpiB) from Streptococcus pyogenes.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2019-03-22 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 68.251, 50.532, 106.977 |
| Unit cell angles | 90.00, 92.32, 90.00 |
Refinement procedure
| Resolution | 27.120 - 1.280 |
| R-factor | 0.1602 |
| Rwork | 0.158 |
| R-free | 0.19550 |
| Structure solution method | SAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.409 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.300 |
| High resolution limit [Å] | 1.280 | 1.280 |
| Rmerge | 0.079 | 0.799 |
| Rmeas | 0.085 | 0.855 |
| Rpim | 0.030 | 0.303 |
| Number of reflections | 92003 | 4451 |
| <I/σ(I)> | 37.1 | 3 |
| Completeness [%] | 98.3 | 96.5 |
| Redundancy | 7.9 | 7.7 |
| CC(1/2) | 0.910 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 292 | Protein: 8.8 mg/ml, 0.01M Tris HCl (pH 8.3);Screen: Classics II (D10), 0.1M Bis-Tris (pH 6.5), 20% (w/v) PEG5000 MME. |
