1G50
CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9 ANGSTROM RESOLUTION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 1997-04-01 |
| Wavelength(s) | 0.9934 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 105.500, 105.500, 136.080 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 * - 2.900 |
| R-factor | 0.241 |
| Rwork | 0.241 |
| R-free | 0.31000 |
| Starting model (for MR) | 1qkt |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | |
| High resolution limit [Å] | 2.900 | 2.900 * |
| Rmerge | 0.080 * | |
| Number of reflections | 18142 | |
| Completeness [%] | 91.0 | 78 * |
| Redundancy | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.3 * | 4 * | PEG400, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 10 | 1 | reservoir | PEG400 | 4-20 (%) | |
| 11 | 1 | reservoir | 350-950 (mM) | ||
| 12 | 1 | reservoir | imidazole | 50 (mM) | |
| 13 | 1 | reservoir | beta-mercaptoethanol | 50 (mM) | |
| 2 | 1 | drop | 50 (mM) | ||
| 3 | 1 | drop | Tris-maleate/HCl | 50 (mM) | pH8. |
| 4 | 1 | drop | estradiol | 0.010 (mM) | |
| 5 | 1 | drop | beta-mercaptoethanol | 50 (mM) | |
| 6 | 1 | drop | PEG400 | 2-10 (%) | |
| 7 | 1 | drop | 400 (mM) | ||
| 8 | 1 | drop | beta-mercaptoethanol | 50 (mM) | |
| 9 | 1 | drop | imidazole | 50 (mM) | pH7.3 |
