7KP2
High Resolution Crystal Structure of Putative Pterin Binding Protein (PruR) from Vibrio cholerae O1 biovar El Tor str. N16961 in Complex with Neopterin
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 | 2019-07-24 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 33.488, 54.616, 33.448 |
| Unit cell angles | 90.00, 91.50, 90.00 |
Refinement procedure
| Resolution | 21.480 - 1.030 |
| R-factor | 0.1286 |
| Rwork | 0.128 |
| R-free | 0.14670 |
| Structure solution method | SAD |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.271 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.050 |
| High resolution limit [Å] | 1.030 | 1.030 |
| Rmerge | 0.092 | 0.764 |
| Rmeas | 0.105 | 0.867 |
| Rpim | 0.049 | 0.404 |
| Number of reflections | 57114 | 2778 |
| <I/σ(I)> | 22.1 | 3.2 |
| Completeness [%] | 96.5 | 93.4 |
| Redundancy | 4.6 | 4.3 |
| CC(1/2) | 0.719 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 292 | Protein: 8.8 mg/ml, 0.01M Tris pH 8.3, 2mM Neopterin; Screen: Classics II (D11), 0.1M Bis-Tris pH 6.5, 28% (w/v) PEG 2000 MME |
