Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-06-05 |
Detector | MARRESEARCH |
Wavelength(s) | 0.933 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.596, 53.638, 104.690 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.650 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.200 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.710 | 1.600 |
High resolution limit [Å] | 1.560 | 1.560 |
Rmerge | 0.038 | 0.139 |
Number of reflections | 34332 | 1069 * |
<I/σ(I)> | 19.13 | |
Completeness [%] | 91.7 * | 39.7 |
Redundancy | 3.7 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 20 * | Tris 0.1 M, PEG 6K 30%, NaCl 0.4 M, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2.3-20 (mg/ml) | |
2 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
3 | 1 | reservoir | 0.5 (M) | ||
4 | 1 | reservoir | PEG6000 |