1HBK
Acyl-CoA binding protein from Plasmodium falciparum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7A |
Temperature [K] | 100 |
Collection date | 1999-11-15 |
Spacegroup name | P 43 |
Unit cell lengths | 48.665, 48.665, 48.411 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.850 - 2.000 |
R-factor | 0.198 |
Rwork | 0.198 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 20.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 * | 1.970 |
High resolution limit [Å] | 2.000 * | 2.000 * |
Rmerge | 0.058 * | 0.516 * |
Total number of observations | 28439 * | |
Number of reflections | 7754 * | 736 * |
<I/σ(I)> | 15.1 | 1.9 |
Completeness [%] | 99.7 | 95.3 * |
Redundancy | 3.2 | 3.4 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | 20 * | pH 8.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | drop | HEPES | 50 (mM) | |
3 | 1 | drop | 300 (mM) | ||
4 | 1 | reservoir | 10 (mM) | ||
5 | 1 | reservoir | Tris | 100 (mM) | |
6 | 1 | reservoir | PEG2000 MME | 20 (%) |