39MR
The crystal structure of a solute-binding protein (N280D mutant) from Trichormus variabilis ATCC 29413 in complex with tryptophan.
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 | 2013-12-15 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 61 |
| Unit cell lengths | 114.406, 114.406, 55.624 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.600 - 1.780 |
| R-factor | 0.2011 |
| Rwork | 0.200 |
| R-free | 0.22710 |
| Structure solution method | SAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.828 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (2.1_6048) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.000 | 1.810 |
| High resolution limit [Å] | 1.780 | 1.780 |
| Rmerge | 0.065 | 0.689 |
| Rpim | 0.020 | 0.215 |
| Number of reflections | 39940 | 1982 |
| <I/σ(I)> | 11.1 | 11 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 11.1 | 11 |
| CC(1/2) | 0.997 | 0.917 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 289 | 0.17 M Ammonium Acetate, 0.085 M Sodium Acetate:HCl, 25.5% (w/v) PEG 4000 and 15% (v/v) Glycerol and 10 mM Tryptophan. |
