4KZK
The structure of the periplasmic L-arabinose binding protein from Burkholderia thailandensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-03-10 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97857 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.770, 51.820, 59.220 |
Unit cell angles | 90.00, 107.34, 90.00 |
Refinement procedure
Resolution | 43.730 - 1.500 |
R-factor | 0.1708 |
Rwork | 0.170 |
R-free | 0.19250 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5abp |
RMSD bond length | 0.008 |
RMSD bond angle | 1.272 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.5.2) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 43.730 | 2.000 | |
High resolution limit [Å] | 1.500 | 8.720 | 1.950 |
Rmerge | 0.111 | 0.038 | 0.437 |
Number of reflections | 11596 | 178 | 836 |
<I/σ(I)> | 21.42 | 47.33 | 6.75 |
Completeness [%] | 100.0 | 98.3 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 50% MPD, 200mM Ammonium Phosphate, 100mM Tris pH8.5, 14.8mg/ml, VAPOR DIFFUSION, SITTING DROP, temperature 298K |