5HQJ
Crystal structure of ABC transporter Solute Binding Protein B1G1H7 from Burkholderia graminis C4D1M, target EFI-511179, in complex with D-arabinose
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 | 2015-10-20 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9793 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.094, 37.403, 62.429 |
Unit cell angles | 90.00, 113.61, 90.00 |
Refinement procedure
Resolution | 27.991 - 1.550 |
R-factor | 0.2081 |
Rwork | 0.206 |
R-free | 0.25400 |
Structure solution method | SAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.355 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | MLPHARE |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.610 |
High resolution limit [Å] | 1.550 | 3.340 | 1.550 |
Rmerge | 0.057 | 0.033 | 0.656 |
Rmeas | 0.061 | 0.035 | 0.705 |
Rpim | 0.022 | 0.013 | 0.258 |
Total number of observations | 282195 | ||
Number of reflections | 37889 | ||
<I/σ(I)> | 10.3 | ||
Completeness [%] | 99.9 | 98.7 | 100 |
Redundancy | 7.4 | 7.2 | 7.4 |
CC(1/2) | 0.998 | 0.910 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | Protein (10 mM HEPES pH 7.5, 5 mM DTT, 10 mM D-Arabinose); Reservoir (MCSG2 B2)(0.2 M Potassium Acetate 20 %(w/v) PEG 3350); Cryoprotection (20% Ethylene Glycol, 80% Reservoir) |