4AH9
Parallel screening of a low molecular weight compound library: do differences in methodology affect hit identification
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-03-20 |
Detector | ADSC QUANTUM 210 |
Spacegroup name | P 31 |
Unit cell lengths | 70.595, 70.595, 66.637 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 61.080 - 1.700 |
R-factor | 0.16823 |
Rwork | 0.166 |
R-free | 0.20882 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bi4 |
RMSD bond length | 0.025 |
RMSD bond angle | 2.640 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.000 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.080 | 0.750 |
Number of reflections | 40414 | |
<I/σ(I)> | 14.2 | 1.7 |
Completeness [%] | 98.8 | 92.2 |
Redundancy | 5.3 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.5 | 100 MM SODIUM ACETATE PH 5.0 TO 5.5, 1.2 M TO 1.5 M AMMONIUM SULFATE. THE PROTEIN WAS IN 40 MM TRIS PH 8.0, 250 MM NACL, 30 MM MGCL2, 5 MM DTT. FRAGMENTS WERE SOAKED INTO PREFORMED CRYSTALS 24-48 HOURS PRIOR TO DATA COLLECTION. |