1TSF
Crystal Structure of the Archaeal homolog of Human RNase P Protein Rpp29 from Archaeoglobus fulgidus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-12-12 |
Detector | MARRESEARCH |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 39.565, 43.790, 49.235 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.700 |
R-factor | 0.25 |
Rwork | 0.250 |
R-free | 0.28300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ts9 |
RMSD bond length | 0.005 |
RMSD bond angle | 1.360 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.760 |
High resolution limit [Å] | 1.670 | 1.700 |
Number of reflections | 8583 | |
Completeness [%] | 87.2 | 98.5 |
Redundancy | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 298 | Sodium Acetate, Ammonium Sulfate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |