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 |