1OC9
TRYPAREDOXIN II FROM C.FASCICULATA solved by MR
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-03-15 |
Detector | MARRESEARCH |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 114.296, 114.296, 101.973 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.350 |
R-factor | 0.19716 |
Rwork | 0.196 |
R-free | 0.21300 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1oc8 |
RMSD bond length | 0.021 * |
RMSD bond angle | 1.650 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.390 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.053 | 0.249 |
Total number of observations | 136117 * | |
Number of reflections | 28025 | |
<I/σ(I)> | 29.8 | 9.6 |
Completeness [%] | 97.5 | 99.9 |
Redundancy | 4.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | pH 7.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | sodium citrate | 500 (mM) | |
3 | 1 | reservoir | HEPES | 30 (mM) | pH7.5 |
4 | 1 | reservoir | dithiothreitol | 5 (mM) |