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 |
