1BA2
D67R MUTANT OF D-RIBOSE-BINDING PROTEIN FROM ESCHERICHIA COLI
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 90 |
Detector technology | IMAGE PLATE |
Collection date | 1996-03 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.801, 89.944, 112.276 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.000 - 2.100 |
R-factor | 0.199 * |
Rwork | 0.199 |
R-free | 0.27900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | SEARCH MODELS REPRESENTING ALL NON-HYDROGEN ATOMS FROM DOMAIN 1 (RESIDUES 1-103 AND 236-264) AND DOMAIN 2 (RESIDUES 104-235 AND 265-271) OF PDB ENTRY 2DRI WERE USED SEPARATELY. |
RMSD bond length | 0.007 * |
RMSD bond angle | 1.850 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.000 | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.038 | 0.097 |
Number of reflections | 27352 | |
<I/σ(I)> | 21.3 | 7.6 |
Completeness [%] | 94.9 | 70 |
Redundancy | 3.36 | 2.04 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7 | VAPOR DIFFUSION OF DROPS CONTAINING 7.5 MG/ML PROTEIN AGAINST A RESERVOIR OF 24% PEG4000, 100 MM TRIS-HCL, PH 7., pH 7.0, vapor diffusion |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7.5 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 24 (%) | |
3 | 1 | reservoir | Tris-HCl | 100 (mM) |