4NV3
The crystal structure of a solute-binding protein (N280D mutant) from Anabaena variabilis ATCC 29413 in complex with valine.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-11-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97883 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 98.869, 100.932, 150.445 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.117 - 1.090 |
| R-factor | 0.1286 |
| Rwork | 0.128 |
| R-free | 0.14280 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4NOR |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.146 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.200 | 1.100 |
| High resolution limit [Å] | 1.090 | 1.090 |
| Rmerge | 0.068 | 0.546 |
| Number of reflections | 308341 | |
| <I/σ(I)> | 32.9 | 1.89 |
| Completeness [%] | 99.4 | 88.9 |
| Redundancy | 5.7 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 289 | 0.1M Sodium Citrate:HCl, 20% (v/v)2-Propanol, 20% (w/v) PEG4000, 10mM Valine., pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
