4LN5
Crystal structure of a trap periplasmic solute binding protein from burkholderia ambifaria (Bamb_6123), TARGET EFI-510059, with bound glycerol and chloride ion
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 | 2013-07-02 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9793 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 96.098, 97.340, 58.115 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.670 - 2.100 |
R-factor | 0.1574 |
Rwork | 0.154 |
R-free | 0.21990 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pfy |
RMSD bond length | 0.007 |
RMSD bond angle | 1.031 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.20) |
Phasing software | BALBES |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 68.386 | 58.115 | 2.210 |
High resolution limit [Å] | 2.100 | 6.640 | 2.100 |
Rmerge | 0.136 | 0.049 | 0.668 |
Total number of observations | 3632 | 16018 | |
Number of reflections | 16289 | ||
<I/σ(I)> | 11.3 | 12.1 | 1.2 |
Completeness [%] | 100.0 | 98.9 | 100 |
Redundancy | 7.2 | 6.4 | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 298 | Protein (16.23 mg/ml, 10 mM HEPES pH 7.5, 150mM NaCl, 5% glycerol, 5 mM DTT), Reservoir (0.8 M Lithium Chloride, 0.1 M Tris pH 8.5, 32%(w/v) PEG 4000 (MCSG1 C9)), Cryoprotection (20% Reservoir, 80% of 50% PEG3350), sitting drop vapor diffusion, temperature 298K |