1OEW
ATOMIC RESOLUTION STRUCTURE OF NATIVE ENDOTHIAPEPSIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-06-15 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.720, 74.660, 42.550 |
Unit cell angles | 90.00, 97.27, 90.00 |
Refinement procedure
Resolution | 42.300 * - 0.910* |
R-factor | 0.121 |
R-free | 0.14700 |
Structure solution method | OTHER |
RMSD bond length | 0.015 |
RMSD bond angle | 0.029 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELXL-97 |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.300 | 0.960 |
High resolution limit [Å] | 0.910 | 0.910 |
Rmerge | 0.109 | 0.503 |
Number of reflections | 186749 | |
<I/σ(I)> | 8.6 | 3 |
Completeness [%] | 99.4 | 99.4 |
Redundancy | 4.7 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 4.6 | BATCH METHOD WITH ENZYME AT A CONCENTRATION OF 2 MG/ML IN 100 MM SODIUM ACETATE BUFFER AT PH 4.6 (MOEWS AND BUNN, 1970) CRYSTALS LEFT TO GROW FOLLOWING SLOW ADDITION OF AMMONIUM SULPHATE TO FINAL CONCENTRATION OF 0.35 G/ML (55% SATURATION). |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 2 (mg/ml) | |
2 | 1 | 1 | sodium acetate | 100 (mM) | pH4.6 |
3 | 1 | 1 | ammonium sulfate | 55 (%sat) |