2V5G
Crystal structure of the mutated N263A YscU C-terminal domain
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X12 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-06-26 |
Detector | MARRESEARCH |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 66.297, 66.297, 68.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.840 - 2.000 |
R-factor | 0.222 |
Rwork | 0.221 |
R-free | 0.25300 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.015 |
RMSD bond angle | 1.756 |
Data reduction software | MOSFLM |
Data scaling software | SCALEPACK |
Phasing software | Auto-Rickshaw |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.110 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.070 | 0.350 |
Number of reflections | 10836 | |
<I/σ(I)> | 8.1 | 2.2 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 13.6 | 13.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | HANGING DROP METHOD USING 3 UL OF A 8 MG/ML PROTEIN SOLUTION MIXED WITH 3UL RESERVOIR BUFFER (1.6 M (NH4)2SO4, 0.2 M NACL, 0.1 M HEPES PH 7.5) IN THE DROPLET. |