3HL8
Crystal structure of exonuclease I in complex with inhibitor BCBP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-21 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97869 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.823, 91.966, 106.280 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.910 - 1.550 |
| R-factor | 0.1739 |
| Rwork | 0.172 |
| R-free | 0.20709 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3c95 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.361 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.071 | 0.360 |
| Number of reflections | 72323 | |
| <I/σ(I)> | 34.5 | 2.69 |
| Completeness [%] | 93.0 | 85.9 |
| Redundancy | 5.7 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 20 mg/mL Protein, 18-27% PEG 4000, 0.1-0.15 M MgCl2, Saturated inhibitor in DMSO soaked 4-5 days, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
