4DT4
Crystal structure of the PPIase-chaperone SlpA with the chaperone binding site occupied by the linker of the purification tag
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-06-23 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.93927 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 40.120, 29.230, 60.690 |
Unit cell angles | 90.00, 93.20, 90.00 |
Refinement procedure
Resolution | 34.310 - 1.350 |
R-factor | 0.16126 |
Rwork | 0.160 |
R-free | 0.20107 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.027 |
RMSD bond angle | 2.297 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.430 |
High resolution limit [Å] | 1.350 | 1.350 |
Number of reflections | 29909 | |
Completeness [%] | 95.5 | 93.8 |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 277 | 28% PEG 3350, 6% MPD (2-methyl-2,4-pentane diol), 100 mM MgCl2 and 100 mM Bis-Tris pH 6, VAPOR DIFFUSION, SITTING DROP, temperature 277K |