Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-12-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.342, 72.932, 73.838 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 51.990 - 2.310 |
R-factor | 0.211 |
Rwork | 0.208 |
R-free | 0.26900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.014 |
RMSD bond angle | 1.497 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.17) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 51.990 | 2.440 |
High resolution limit [Å] | 2.310 | 2.310 |
Rmerge | 0.078 | 0.233 |
Number of reflections | 11954 | |
<I/σ(I)> | 13.3 | 5.3 |
Completeness [%] | 90.6 | 84.8 |
Redundancy | 2.5 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | PROTEIN AT 10MG/ML WELL BUFFER CONTAINING 17.5% PEG3350, 200MM HEPES, PH7.0, 100MM AMMONIUM ACETATE, pH 7.00 |