3KXC
Mutant transport protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-03-05 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97852 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 48.172, 69.265, 121.376 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.280 - 2.000 |
R-factor | 0.19799 |
Rwork | 0.196 |
R-free | 0.23238 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cfh |
RMSD bond length | 0.009 |
RMSD bond angle | 1.115 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 26752 | |
<I/σ(I)> | 16.8 | 3 |
Completeness [%] | 94.9 | 87.6 |
Redundancy | 4.05 | 4.15 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 22% PEG 3350, 0.2M Li2SO4, 0.1M Bis-Tris, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |