4UT1
The structure of the flagellar hook junction protein FlgK from Burkholderia pseudomallei
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Collection date | 2013-10-24 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.597, 113.005, 62.234 |
| Unit cell angles | 90.00, 106.08, 90.00 |
Refinement procedure
| Resolution | 39.969 - 1.800 |
| R-factor | 0.1999 |
| Rwork | 0.198 |
| R-free | 0.24400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.927 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | BALBES |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.120 | 0.660 |
| Number of reflections | 49944 | |
| <I/σ(I)> | 14.9 | 2.4 |
| Completeness [%] | 97.8 | 96.8 |
| Redundancy | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 0.1M SUCCINIC ACID PH 7.0, 15% PEG 3350 |
