1JO8
Structural analysis of the yeast actin binding protein Abp1 SH3 domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-09-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.842 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 24.080, 38.155, 59.090 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 17.510 - 1.300 |
| R-factor | 0.14512 |
| Rwork | 0.144 |
| R-free | 0.17785 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cka |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.714 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 * | 1.320 |
| High resolution limit [Å] | 1.300 | 1.300 |
| Rmerge | 0.056 | 0.266 |
| Total number of observations | 56424 * | |
| Number of reflections | 13742 * | |
| <I/σ(I)> | 20.3 | 4 |
| Completeness [%] | 98.0 | 88.6 |
| Redundancy | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 298 | Ammonium sulfate, bis-tris-propane, pH 8.0, VAPOR DIFFUSION, SITTING DROP at 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium sulfate | 3.2 (M) | |
| 2 | 1 | reservoir | Bis-Tris propane | 100 (mM) | pH8.0 |
| 3 | 1 | drop | Abp1-SH3 | 12 (mg/ml) |
