39LS
The crystal structure of a solute-binding protein (N280D mutant) from Trichormus variabilis ATCC 29413 in complex with Phenylalanine.
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 | 2013-11-10 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 61 |
| Unit cell lengths | 114.444, 114.444, 55.493 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 27.490 - 1.800 |
| R-factor | 0.1985 |
| Rwork | 0.197 |
| R-free | 0.22110 |
| Structure solution method | SAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.795 |
| 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] | 28.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.077 | 0.675 |
| Rpim | 0.028 | 0.253 |
| Number of reflections | 38576 | 1916 |
| <I/σ(I)> | 38.3 | 3 |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 6.9 | 7 |
| CC(1/2) | 0.994 | 0.802 |
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 |
