1E9N
A second divalent metal ion in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1, and its implications for the catalytic mechanism
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 1999-07-15 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 137.522, 45.016, 125.702 |
| Unit cell angles | 90.00, 108.03, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| Rwork | 0.186 |
| R-free | 0.25200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | TO BE PUBLISHED |
| RMSD bond length | 0.018 |
| RMSD bond angle | 18.920 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | EPMR |
| Refinement software | TNT (5F) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 67.420 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.082 * | 0.379 |
| Total number of observations | 102875 * | |
| Number of reflections | 34905 | |
| <I/σ(I)> | 11.8 | 2.1 |
| Completeness [%] | 93.0 | 70.5 |
| Redundancy | 2.9 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 4 * | HANGING DROP, DROP 2+2 UL, 15MG/ML PROTEIN, 1 ML WELL, 0.1M TRIS-HCL, PH 7.5, 0.2M NAOAC, 30% PEG4K, 20MM HECAMEG, 1MM PB(OAC)2, 1MM DTT |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-12 (mg/ml) | |
| 2 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 3 | 1 | reservoir | sodium acetate | 0.2 (M) | |
| 4 | 1 | reservoir | PEG4000 | 25 (%) | |
| 5 | 1 | reservoir | lead (II) acetate | 1 (mM) | |
| 6 | 1 | reservoir | HECAMEG | 19.5 (mM) |
