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) |






