1RKM
STRUCTURE OF OPPA
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.5 |
Synchrotron site | SRS |
Beamline | PX9.5 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1995-07-08 |
Detector | MARRESEARCH |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 97.840, 97.840, 137.210 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.400 |
R-factor | 0.191 * |
Rwork | 0.191 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | OLIGOPEPTIDE BINDING PROTEIN PDB CODE 2OLB |
RMSD bond length | 0.018 |
RMSD bond angle | 0.049 |
Data reduction software | DENZO |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.103 | 0.457 |
Total number of observations | 112007 * | |
Number of reflections | 30015 | |
<I/σ(I)> | 6.8 | 1.6 |
Completeness [%] | 99.3 | 99.5 |
Redundancy | 3.7 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 3M (NH4)2SO4, 0.1M HEPES PH7.5, 0.2M NACL AND 20MG/ML OPPA |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 3 (M) | |
2 | 1 | reservoir | 0.3 (M) | ||
3 | 1 | drop | protein | 30 (mg/ml) | |
4 | 1 | drop | HEPES | 0.1 (M) |