5LIR
Structure of the SALTY Sigma cross-reacting protein 27A (SCRP-27A) from Salmonella typhimurium
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-11 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.873 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 99.662, 99.662, 52.510 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 44.860 - 1.750 |
R-factor | 0.16702 |
Rwork | 0.166 |
R-free | 0.18666 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vhq |
RMSD bond length | 0.023 |
RMSD bond angle | 2.103 |
Data reduction software | XDS (Oct 15, 2015) |
Data scaling software | XDS (Oct 15, 2015) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.860 | 1.800 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.102 | 1.700 |
Number of reflections | 30563 | |
<I/σ(I)> | 11.65 | 0.98 |
Completeness [%] | 100.0 | 99 |
Redundancy | 8.4 | 8.5 |
CC(1/2) | 0.999 | 0.461 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M Sodium acetate pH 4.6 40 % PEG 200 |