3FRN
CRYSTAL STRUCTURE OF flagellar protein FlgA FROM Thermotoga maritima MSB8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 90 |
Detector technology | CCD |
Collection date | 2008-05-09 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9795 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.087, 28.631, 95.530 |
Unit cell angles | 90.00, 106.83, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.050 |
R-factor | 0.24234 |
Rwork | 0.241 |
R-free | 0.28198 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.171 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELX |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.090 |
High resolution limit [Å] | 2.026 | 2.020 |
Rmerge | 0.089 | 0.650 |
Number of reflections | 18429 | |
<I/σ(I)> | 8 | 1.6 |
Completeness [%] | 97.8 | 63 |
Redundancy | 3.8 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 200MM AMMONIUM PHOSPHATE, PH 7.5, 20% PEG3350, 10% GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K |