1DMU
Crystal structure of the restriction endonuclease BglI (e.c.3.1.21.4) bound to its dna recognition sequence
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1997-06-11 |
| Detector | CUSTOM-MADE |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 78.480, 81.600, 117.060 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.200 |
| R-factor | 0.183 |
| Rwork | 0.177 |
| R-free | 0.23900 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.400 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | X-PLOR (3.843) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.250 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.055 | 0.078 |
| Number of reflections | 17679 | |
| <I/σ(I)> | 23.3 | |
| Completeness [%] | 90.8 | 57.1 |
| Redundancy | 3.3 | 0.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 * | 293 | 7-12% PEG 4000, 75-150MM LI2SO4, 100MM TRIS-HCL, 1:2 PROTEIN:DNA MOLAR RATIO, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | LI2SO4 | ||
| 2 | 1 | 1 | TRIS-HCL | ||
| 3 | 1 | 1 | PEG 4000 | ||
| 4 | 1 | 2 | PEG 4000 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | 50 (mM) | ||
| 3 | 1 | drop | Tris-HCl | ||
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | reservoir | PEG4000 | 7-12 (%) | |
| 6 | 1 | reservoir | 75-150 (mM) | ||
| 7 | 1 | reservoir | Tris-HCl | 100 (mM) |
