2G30
beta appendage of AP2 complexed with ARH peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-05-05 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.03 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 37.750, 36.313, 98.982 |
Unit cell angles | 90.00, 92.91, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.600 |
R-factor | 0.216 |
Rwork | 0.215 |
R-free | 0.24300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1e42 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.458 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.450 | 1.690 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.076 | 0.689 |
Number of reflections | 35656 | 5081 |
<I/σ(I)> | 19 | 3.1 |
Redundancy | 5.4 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | 18% PEG 8000, 100mM HEPES pH 7.5, 4mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 289K |