3Q1J
Crystal structure of tudor domain 1 of human PHD finger protein 20
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E |
| Detector technology | IMAGE PLATE |
| Collection date | 2010-10-06 |
| Detector | RIGAKU RAXIS |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 60.498, 41.062, 28.632 |
| Unit cell angles | 90.00, 110.33, 90.00 |
Refinement procedure
| Resolution | 19.080 - 2.350 |
| R-factor | 0.2074 |
| Rwork | 0.205 |
| R-free | 0.26010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb entries 2rhu 2eqm |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.040 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | BUSTER-TNT (BUSTER 2.8.0) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 20.000 | 2.430 |
| High resolution limit [Å] | 2.350 | 5.040 | 2.350 |
| Rmerge | 0.100 | 0.059 | 0.654 |
| Number of reflections | 2828 | ||
| <I/σ(I)> | 9.1 | ||
| Completeness [%] | 99.8 | 99.3 | 100 |
| Redundancy | 3.4 | 3.3 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 25% PEG-3350, 0.2M ammonium acetate, 0.1M bis-tris. Prior to freezing, a cluster of thin rods was transferred to a drop of paratone oil. A fragment of the cluster was frozen in a stream of cold nitrogen., pH 5.5, vapor diffusion, sitting drop, temperature 291K, VAPOR DIFFUSION, SITTING DROP |
