4AFP
The structure of metacaspase 2 from T. brucei determined in the presence of Samarium
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-26 |
Detector | ADSC CCD |
Wavelength(s) | 1.84560, 1.805, 1.846 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 78.217, 49.787, 85.224 |
Unit cell angles | 90.00, 117.10, 90.00 |
Refinement procedure
Resolution | 75.870 - 2.100 |
R-factor | 0.18405 |
Rwork | 0.181 |
R-free | 0.23787 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.009 |
RMSD bond angle | 1.204 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | Auto-Rickshaw |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.290 | 2.210 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.060 | 0.090 |
Number of reflections | 16074 | |
<I/σ(I)> | 21.5 | 10.5 |
Completeness [%] | 93.7 | 68.2 |
Redundancy | 6.6 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 50 MM HEPES PH 7.0, 0.1% TRYPTONE, 20% PEG 3350 |