1DCQ
CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-11-14 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 73.935, 132.208, 59.817 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.100 |
| R-factor | 0.23 |
| Rwork | 0.213 |
| R-free | 0.26600 |
| Structure solution method | MAD |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.460 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.045 | 0.119 |
| Number of reflections | 77917 | |
| <I/σ(I)> | 24.6 | |
| Completeness [%] | 99.1 | 97.8 |
| Redundancy | 4.6 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.5 | 20 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 30 (%) | |
| 3 | 1 | reservoir | sodium acetate | 0.2 (M) | |
| 4 | 1 | reservoir | Tris-HCl | 0.1 (M) |
