4NE4
Crystal structure of ABC transporter substrate binding protein ProX from Agrobacterium tumefaciens cocrystalized with BTB
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97929 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.888, 64.388, 100.746 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.730 |
| R-factor | 0.1533 |
| Rwork | 0.152 |
| R-free | 0.18650 |
| Structure solution method | SAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.149 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXS |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.760 |
| High resolution limit [Å] | 1.730 | 4.690 | 1.730 |
| Rmerge | 0.083 | 0.054 | 0.459 |
| Number of reflections | 31774 | ||
| <I/σ(I)> | 10 | ||
| Completeness [%] | 100.0 | 99.4 | 100 |
| Redundancy | 7.9 | 7.3 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | PEG3350 25%, Li-Sulfate 0.2M, Bis-Tris 0.1M, pH 5.5, vapor diffusion, sitting drop, temperature 293K |
