4OAT
The crystal structure of a solute-binding protein (N280D mutant) from Anabaena variabilis ATCC 29413 in complex with isoleucine.
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 | 2013-11-27 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97918 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 97.912, 101.179, 149.577 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.488 - 1.199 |
| R-factor | 0.1302 |
| Rwork | 0.129 |
| R-free | 0.14990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nqr |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.123 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.500 | 1.220 |
| High resolution limit [Å] | 1.199 | 1.200 |
| Rmerge | 0.072 | 0.360 |
| Number of reflections | 226601 | |
| <I/σ(I)> | 39.5 | 4.5 |
| Completeness [%] | 98.3 | 84.6 |
| Redundancy | 5.8 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | 0.2 M Sodium Chloride, 0.1 M Bis-Tris:HCl, 25% (w/v) PEG 3350, 10 mM Isoleucine, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
