1BH8
HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE
Experimental procedure
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM02 |
Synchrotron site | ESRF |
Beamline | BM02 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-01 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.400, 48.400, 77.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 3.000 |
R-factor | 0.199 |
Rwork | 0.199 |
R-free | 0.28200 |
Structure solution method | MIR |
RMSD bond length | 0.007 |
RMSD bond angle | 1.450 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SHARP |
Refinement software | CNS (0.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.039 * | 0.115 * |
Total number of observations | 9480 * | |
Number of reflections | 3376 | |
<I/σ(I)> | 21.6 | 12.8 |
Completeness [%] | 82.0 | 78.1 |
Redundancy | 2.8 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.9 * | 4 * | drop solution was mixed with an equal volume of reservoir solution * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8-15 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 10 (mM) | |
3 | 1 | reservoir | PEG4000 | 10 (%) | |
4 | 1 | reservoir | ammonium sulfate | 100 (mM) | |
5 | 1 | reservoir | HEPES |