5IM2
Crystal structure of a TRAP solute binding protein from Rhodoferax ferrireducens T118 (Rfer_2570, TARGET EFI-510210) in complex with copurified benzoate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-04-09 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.014, 71.864, 78.603 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.568 - 1.700 |
| R-factor | 0.1594 |
| Rwork | 0.157 |
| R-free | 0.19920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5i7i |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.979 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.1.27) |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 28.570 | 28.570 | 1.730 |
| High resolution limit [Å] | 1.700 | 9.000 | 1.700 |
| Rmerge | 0.121 | 0.049 | 0.717 |
| Rmeas | 0.130 | 0.054 | 0.777 |
| Rpim | 0.049 | 0.022 | 0.297 |
| Total number of observations | 224541 | 853 | 11514 |
| Number of reflections | 32423 | ||
| <I/σ(I)> | 7.9 | 13.2 | 1.8 |
| Completeness [%] | 99.7 | 64.9 | 100 |
| Redundancy | 6.9 | 5 | 6.8 |
| CC(1/2) | 0.996 | 0.998 | 0.801 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 298 | Protein (10 mM HEPES pH 7.5, 5 mM DTT, 10 mM 3,4-Dihydroxybenzoate); Reservoir (MCSG1 D12, 0.2 M Ammonium Chloride pH 6.3, 20 %(w/v) PEG 3350); Cryoprotection (20% diethylen glycol, 80% reservoir) |
