1BAZ
ARC REPRESSOR MUTANT PHE10VAL
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1993-10 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 91.900, 52.570, 47.320 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 1.900 |
R-factor | 0.213 |
Rwork | 0.213 |
R-free | 0.27300 |
RMSD bond length | 0.012 |
RMSD bond angle | 21.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 1.970 | |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.087 | |
Number of reflections | 16796 | |
Completeness [%] | 89.9 * | 50.7 |
Redundancy | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | PROTEIN WAS CRYSTALLIZED FROM 40-45% SATURATED AMMONIUM PHOSPHATE, PH 8.0, BY MACROSEEDING USING CRYSTALS OF THE WILD TYPE PROTEIN |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | ammonium phosphate | 55 (%sat) |