1EWR
CRYSTAL STRUCTURE OF TAQ MUTS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-05-01 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 96.734, 96.734, 427.126 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.940 - 3.190 |
R-factor | 0.331 |
Rwork | 0.331 |
R-free | 0.36100 |
RMSD bond length | 0.010 |
RMSD bond angle | 22.400 * |
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 | 3.250 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmerge | 0.067 | 0.443 |
Number of reflections | 30381 | |
<I/σ(I)> | 16.1 | |
Completeness [%] | 88.6 | 85.3 |
Redundancy | 4.3 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 27 * | PEG 400, ammonium sulfate, copper chloride, HEPES, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 40 (mg/ml) | |
10 | 1 | reservoir | ammonium sulfate | 1.8 (M) | |
11 | 1 | reservoir | 1.5 (mM) | ||
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | drop | 200 (mM) | ||
4 | 1 | drop | dithiothreitol | 1 (mM) | |
5 | 1 | d | EDTA | 0.1 (mM) | |
6 | 1 | drop | 5 (mM) | ||
7 | 1 | drop | glycerol | 5 (%) | |
8 | 1 | reservoir | HEPES | 90 (mM) | |
9 | 1 | reservoir | PEG400 | 7.2 (%) |