1JEU
OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH KEK
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 111.410, 76.410, 71.250 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.250 |
| R-factor | 0.224 * |
| Rwork | 0.224 |
| R-free | 0.25200 |
| Starting model (for MR) | 2olb |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.020 |
| Data reduction software | DENZO |
| Phasing software | CCP4 |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | |
| High resolution limit [Å] | 1.250 | |
| Rmerge | 0.044 | |
| Number of reflections | 167630 | |
| <I/σ(I)> | 9 | |
| Completeness [%] | 97.8 | 93.2 * |
| Redundancy | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 5.5 | Tame, J.R., (1994) Science, 264, 1578. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | 50 (mM) | ||
| 2 | 1 | 1 | PEG4000 | 15 (%) | |
| 3 | 1 | 1 | uranyl acetate | 1 (mM) |
