3DNU
structure of MDT protein
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-04-12 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9797, 1.02, 0.9796 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 48.660, 85.810, 49.670 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.990 - 1.540 |
R-factor | 0.195 |
Rwork | 0.195 |
R-free | 0.23200 |
Structure solution method | MAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.600 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.000 | 1.640 |
High resolution limit [Å] | 1.540 | 1.540 |
Rmerge | 0.054 | 0.380 |
Number of reflections | 59003 | |
<I/σ(I)> | 13.7 | 2 |
Completeness [%] | 98.0 | |
Redundancy | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | peg 8000, glycerol, phosphate buffer, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |