1URU
Amphiphysin BAR domain from Drosophila
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-11-15 |
Detector | ADSC CCD |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 49.586, 49.586, 190.319 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 63.250 - 2.600 |
R-factor | 0.23 * |
Rwork | 0.236 |
R-free | 0.30636 |
Structure solution method | OTHER |
RMSD bond length | 0.013 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHARP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.940 | 2.740 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.134 | 0.010 * |
Number of reflections | 8657 | |
<I/σ(I)> | 4.9102 | 0.73 |
Completeness [%] | 97.2 | 86 |
Redundancy | 10.21 | 9.29 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.4 * | 2.5MG/ML PROTEIN SOLUTION IN 18% PEG4000, 200MM NACL, 1MM DTT, 20MM HEPES PH 7.4 MIXED WITH THE WELL SOLUTION 18% PEG 4000, 0.2M AMMONIUM ACETATE, 100MM SODIUM CITRATE PH 6.0. CRYSTALS WERE EQUILIBRATED IN 20% GLYCEROL FOR COOLING TO 100K. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2.5 (mg/ml) | |
2 | 1 | drop | PEG4000 | 18 (%) | |
3 | 1 | drop | 200 (mM) | ||
4 | 1 | drop | dithiothreitol | 1 (mM) | |
5 | 1 | drop | HEPES | 20 (mM) | |
6 | 1 | reservoir | PEG4000 | 18 (%) | |
7 | 1 | reservoir | ammonium acetate | 0.2 (M) | |
8 | 1 | reservoir | sodium citrate | 100 (mM) |