1IBW
STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT 25 C
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-06-21 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 97.017, 117.768, 205.789 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.200 |
| R-factor | 0.21086 |
| Rwork | 0.204 |
| R-free | 0.26900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pya |
| RMSD bond length | 0.015 |
| RMSD bond angle | 2.420 |
| 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] | 20.000 | 3.310 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.103 | 0.454 |
| Number of reflections | 15945 | |
| <I/σ(I)> | 10.7 | |
| Completeness [%] | 80.7 | 84.8 |
| Redundancy | 1.8 | 1.8 |
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 |
