3FLG
The PWWP domain of Human DNA (cytosine-5-)-methyltransferase 3 beta
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E DW |
| Temperature [K] | 100 |
| Wavelength(s) | 1.54178 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 54.170, 75.062, 34.488 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.940 - 1.800 |
| R-factor | 0.206 |
| Rwork | 0.204 |
| R-free | 0.24400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1khc |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.482 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 3.880 | 1.800 |
| Rmerge | 0.059 | 0.056 | 0.123 |
| Number of reflections | 13589 | ||
| <I/σ(I)> | 22.974 | ||
| Completeness [%] | 99.7 | 98.9 | 100 |
| Redundancy | 6.8 | 6.5 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | Purified DNMT3B was crystallized using sitting drop vapor diffusion method at 20 C by mixing 1 ul of the protein solution with 1 ul of the reservoir solution containing 30% PEG 2,000 MME, 0.2 M KBr, pH 7.5, VAPOR DIFFUSION, HANGING DROP |
