2QEL
Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-11-14 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.115 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 58.360, 58.360, 229.160 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.290 |
R-factor | 0.234 |
Rwork | 0.231 |
R-free | 0.28900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1g1o |
RMSD bond length | 0.015 |
RMSD bond angle | 1.567 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 76.472 | 29.180 | 2.420 |
High resolution limit [Å] | 2.290 | 7.250 | 2.290 |
Rmerge | 0.114 | 0.031 | 0.554 |
Total number of observations | 6869 | 24773 | |
Number of reflections | 20038 | ||
<I/σ(I)> | 3.1 | 19.7 | 1.4 |
Completeness [%] | 93.9 | 98 | 92 |
Redundancy | 9.9 | 8.9 | 8.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 0.1M Tris, 2.4M Ammonium sulphate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |