4NVE
Predicting protein conformational response in prospective ligand discovery
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-11-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.11587 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.880, 73.530, 104.320 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.830 - 1.540 |
| R-factor | 0.1468 |
| Rwork | 0.145 |
| R-free | 0.17960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.459 |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.830 | 1.580 |
| High resolution limit [Å] | 1.540 | 1.540 |
| Rmerge | 0.386 | |
| Number of reflections | 54804 | |
| <I/σ(I)> | 2.2 | |
| Completeness [%] | 93.5 | 62 |
| Redundancy | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 283 | Compound soaked into crystal grown in equal volume of 500mM MES buffer (pH 6.0) and 25% MPD, vapor diffusion, hanging drop, temperature 283K |
