2RHB
Crystal structure of Nsp15-H234A mutant- Hexamer in asymmetric unit
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-ID-B |
Synchrotron site | APS |
Beamline | 14-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-11-23 |
Detector | MAR CCD 165 mm |
Spacegroup name | H 3 |
Unit cell lengths | 305.757, 305.757, 88.740 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.800 |
R-factor | 0.20043 |
Rwork | 0.198 |
R-free | 0.25953 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2h85 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.067 |
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] | 152.500 | 2.870 |
High resolution limit [Å] | 2.800 | 2.800 |
Number of reflections | 66521 | |
Completeness [%] | 91.9 | 78.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.9 | 289 | at 10-15 mg/ml of protein in 0.05-0.1 M MgCl2, 3-5 % MPD and 0.1 M tri-sodium citrate dehydrate (pH 5.6-5.9). , VAPOR DIFFUSION, HANGING DROP, temperature 289K, pH 5.90 |