2HQX
Crystal structure of human P100 tudor domain conserved region
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-12-25 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.9790 |
| Spacegroup name | P 1 |
| Unit cell lengths | 30.777, 37.684, 40.202 |
| Unit cell angles | 90.03, 105.32, 99.72 |
Refinement procedure
| Resolution | 38.720 - 1.420 |
| R-factor | 0.23163 |
| Rwork | 0.229 |
| R-free | 0.27042 |
| Structure solution method | PT-SAS |
| Starting model (for MR) | 2hqe |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.210 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.720 | 1.460 |
| High resolution limit [Å] | 1.420 | 1.420 |
| Number of reflections | 25303 | |
| <I/σ(I)> | 15.6 | |
| Completeness [%] | 82.2 | 23.08 |
| Redundancy | 3.4 | 1.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MODIFIED MICROBATCH | 7.9 | 291 | 1.0 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN CONCENTRATE (11.0 MG/ML) AND RESERVOIR SOLUTION CONTAINING 1.06M AMMONIUM SULFATE, 200.0 MM LITHIUM SULFATE, 0.1M TRIS PH 7.9, MODIFIED MICROBATCH, temperature 291K |
