1EF0
CRYSTAL STRUCTURE OF PI-SCEI MINIPRECURSOR
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 | 1998-10-01 |
| Detector | RIGAKU RAXIS |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 59.003, 101.683, 86.765 |
| Unit cell angles | 90.00, 93.51, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.100 |
| R-factor | 0.231 |
| Rwork | 0.231 |
| R-free | 0.28100 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 23.600 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 20.000 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.101 | 0.101 |
| Total number of observations | 419279 * | |
| Number of reflections | 61089 * | |
| <I/σ(I)> | 8.6 | |
| Completeness [%] | 93.3 | 93.3 |
| Redundancy | 6.8 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 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 | 31 (mg/ml) | |
| 2 | 1 | reservoir | PEG3350 | 10 (%(w/v)) | |
| 3 | 1 | reservoir | 3 (mM) | ||
| 4 | 1 | reservoir | 1 (mM) | ||
| 5 | 1 | reservoir | beta-mercaptoethanol | 10 (mM) | |
| 6 | 1 | reservoir | Tris-HCl | 100 (mM) |
