4N8Y
Crystal structure of a trap periplasmic solute binding protein from bradyrhizobium sp. btai1 b (bbta_0128), target EFI-510056 (bbta_0128), complex with alpha/beta-d-galacturonate
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 | 2013-10-09 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.971 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.798, 85.705, 86.246 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.087 - 1.500 |
R-factor | 0.1452 |
Rwork | 0.144 |
R-free | 0.17510 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4n17 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.215 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.20) |
Phasing software | AMoRE |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 86.246 | 85.705 | 1.580 |
High resolution limit [Å] | 1.500 | 4.740 | 1.500 |
Rmerge | 0.057 | 0.020 | 0.523 |
Total number of observations | 21173 | 93789 | |
Number of reflections | 90134 | ||
<I/σ(I)> | 22.7 | 29.9 | 1.5 |
Completeness [%] | 96.1 | 95.8 | 94.4 |
Redundancy | 7.5 | 6.9 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | Protein (56.1 mg/ml, 10 mM HEPES, 5 mM DTT, 10 mM D-Galacturonate); Reservoir (0.1 M HEPES, 25 %(w/v) PEG 3350); Cryoprotection (20% Reservoir, 80% PEG3350 (50% w/v)), pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |