261L
STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 298 |
Detector technology | CCD |
Detector | ADSC QUANTUM 1 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 61.125, 61.125, 97.338 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.500 |
R-factor | 0.17 * |
Rwork | 0.170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | CYS-FREE VERSION OF T4-LYSOZYME |
RMSD bond length | 0.010 |
RMSD bond angle | 0.000 * |
Data reduction software | MOSFLM |
Data scaling software | XDS ((SCALA)) |
Phasing software | TNT |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.084 | 0.200 |
Number of reflections | 28161 | |
<I/σ(I)> | 2 | |
Completeness [%] | 86.5 | |
Redundancy | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 | CRYSTALS WERE GROWN FROM 20% POLYETHYLENE GLYCOL 6000, 20% ISOPROPANOL, 50MM TRIS-HCL PH 7.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 20 (mg/ml) | |
2 | 1 | 1 | PEG6000 | 20 (%) | |
3 | 1 | 1 | isopropanol | 20 (%) | |
4 | 1 | 1 | Tris-HCl | 50 (mM) |