1AVQ
TOROIDAL STRUCTURE OF LAMBDA EXONUCLEASE DETERMINED AT 2.4 ANGSTROMS
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 105 |
Detector technology | IMAGE PLATE |
Collection date | 1997-01 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 156.700, 156.700, 131.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.400 |
Rwork | 0.198 |
Structure solution method | MIR WITH ANOMALOUS DISPERSION |
RMSD bond length | 0.017 |
RMSD bond angle | 17.950 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | TNT (5E) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.440 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.055 * | |
Total number of observations | 291671 * | |
Number of reflections | 62855 | |
<I/σ(I)> | 11.9 | 4.7 |
Completeness [%] | 97.0 | 94.3 |
Redundancy | 4.6 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.7 | 277 | PROTEIN WAS CRYSTALLIZED FROM 1.2 M NH2SO4, 0.2 M NACL 0.1 M NAACETATE PH 4.7, AT 4 DEGREES CELSIUS., temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | ammonium salfate | 1.2 (M) | |
2 | 1 | 1 | 0.2 (M) | ||
3 | 1 | 1 | sodium acetate | 0.1 (M) |