1OBD
SAICAR-synthase complexed with ATP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-02-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 61.480, 63.050, 79.820 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.400 |
R-factor | 0.15621 |
Rwork | 0.152 |
R-free | 0.19471 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1a48 |
RMSD bond length | 0.017 * |
RMSD bond angle | 1.861 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.420 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.085 | 0.190 |
Number of reflections | 59985 | |
<I/σ(I)> | 17 | 7 |
Completeness [%] | 97.0 | 97.4 |
Redundancy | 3.5 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 | THE HANGING DROPS CONTAINED PROTEIN AT A CONCENTRATION OF 8 - 15 MG/ML, 50 MM TRIS-HCL BUFFER, PH 7.0, 40 MM ASPARTIC ACID AND 1.0 - 1.25 M AMMONIUM SULPHATE. THE WELL CONTAINED THE SAME ABOVE BUFFER PLUS 2.25 M AMMONIUM SULPHATE |