5CI5
Crystal Structure of an ABC transporter Solute Binding Protein from Thermotoga Lettingae TMO (Tlet_1705, TARGET EFI-510544) bound with alpha-D-Tagatose
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 | 2015-06-26 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9793 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 73.363, 93.077, 103.637 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 26.619 - 1.610 |
R-factor | 0.1337 |
Rwork | 0.132 |
R-free | 0.16790 |
Structure solution method | SAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.290 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.640 |
High resolution limit [Å] | 1.610 | 4.370 | 1.610 |
Rmerge | 0.113 | 0.052 | 0.957 |
Rmeas | 0.117 | 0.054 | 0.992 |
Rpim | 0.030 | 0.014 | 0.261 |
Total number of observations | 1362797 | ||
Number of reflections | 92888 | ||
<I/σ(I)> | 6.2 | ||
Completeness [%] | 100.0 | 99.3 | 100 |
Redundancy | 14.7 | 14.2 | 14.2 |
CC(1/2) | 0.997 | 0.895 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | Protein (10mM D-tagatose, 10 mM HEPES pH 7.5, 5 mM DTT); Reservoir (0.2 M Sodium chloride, 0.1M Bis-Tris HCl, 25%(w/v) PEG 3350); Cryoprotection (20% Diethylene glycol, 80% Reservoir) |