1EQN
E.COLI PRIMASE CATALYTIC CORE
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-06-01 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.98636, 0.97939, 0.97900, 0.96526 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.674, 107.626, 263.069 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 500.000 - 2.900 |
R-factor | 0.2259 |
Rwork | 0.220 |
R-free | 0.27600 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.414 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.058 | 0.207 |
Total number of observations | 273234 * | |
Number of reflections | 40874 * | |
<I/σ(I)> | 31.3 | |
Completeness [%] | 97.6 | 90.8 |
Redundancy | 6.9 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.3 | 20 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 16-19 (%) | |
3 | 1 | reservoir | Tris-HCl | 0.053-0.063 (mM) | |
4 | 1 | reservoir | sodium acetate | 0.11-0.13 (M) |