2VPO
High resolution structure of the periplasmic binding protein TeaA from TeaABC TRAP transporter of Halomonas elongata in complex with hydroxyectoine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-12-06 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 48.600, 52.100, 63.700 |
Unit cell angles | 80.80, 85.70, 78.00 |
Refinement procedure
Resolution | 19.820 - 1.800 |
R-factor | 0.182 |
Rwork | 0.179 |
R-free | 0.22500 |
Structure solution method | OTHER |
Starting model (for MR) | NONE |
RMSD bond length | 0.012 |
RMSD bond angle | 1.411 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | ARP/wARP |
Refinement software | REFMAC (5.4.0069) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.840 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.010 | 0.080 |
Number of reflections | 53752 | |
<I/σ(I)> | 8.8 | 2.3 |
Completeness [%] | 96.2 | 94 |
Redundancy | 3.8 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 100 MM HEPES PH 7.5, 40 MM MGCL2, 35 % PEG 3350 |