1AII
ANNEXIN III
Experimental procedure
Source type | SYNCHROTRON |
Source details | LURE BEAMLINE D41A |
Synchrotron site | LURE |
Beamline | D41A |
Temperature [K] | 300 |
Detector technology | IMAGE PLATE |
Collection date | 1995-06-08 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.290, 68.720, 50.590 |
Unit cell angles | 90.00, 94.27, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.950 |
R-factor | 0.193 * |
Rwork | 0.193 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1axn |
RMSD bond length | 0.009 |
RMSD bond angle | 2.584 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | AMoRE |
Refinement software | PROLSQ |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.950 | 2.000 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.072 * | 0.139 * |
Total number of observations | 78671 * | |
Number of reflections | 20818 | |
<I/σ(I)> | 4.71 | 4.7 |
Completeness [%] | 98.5 | 83.5 |
Redundancy | 2.9 | 2.08 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 * | 18MG/ML PROTEIN, 10MM CACL2 IN 50 MM HEPES AT PH=7.8 WAS EQUILIBRATED AGAINST 50% AMMONIUM SULFATE IN THE SAME BUFFER. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 18 (mg/ml) | |
2 | 1 | drop | 10 (mM) | ||
3 | 1 | drop | 1 (mM) | ||
4 | 1 | drop | inositol 2-phosphate | 1 (mM) | |
5 | 1 | drop | ammonium sulfate | 25 (%) | |
6 | 1 | drop | Tris-HCl | 50 (mM) | |
7 | 1 | reservoir | ammonium sulfate | 50 (%) |