1IBV
STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT-170 C
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 103 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-03-08 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 96.272, 115.480, 206.393 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.500 |
| R-factor | 0.24654 |
| Rwork | 0.243 |
| R-free | 0.27930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pya |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 2.520 |
| High resolution limit [Å] | 2.500 * | 2.430 |
| Rmerge | 0.073 | 0.336 |
| Number of reflections | 39581 | |
| <I/σ(I)> | 19.1 | |
| Completeness [%] | 91.4 | 93.2 |
| Redundancy | 2.9 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | PEG 400, PEG 4000, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | reservoir | PEG400 | 0-15 (%) | |
| 3 | 1 | reservoir | PEG4000 | 4-8 (%) | |
| 4 | 1 | reservoir | sodium acetate | 0.1 (M) | pH4.6 |
