2AAG
Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-01-06 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 57.709, 82.105, 77.603 |
| Unit cell angles | 90.00, 101.15, 90.00 |
Refinement procedure
| Resolution | 19.210 - 1.850 |
| R-factor | 0.181 |
| Rwork | 0.178 |
| R-free | 0.23178 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | c-alpha trace of density map resulting from a single-wavelength anomalous difference data set (using Hg's anomalous signal) |
| RMSD bond length | 0.028 |
| RMSD bond angle | 2.325 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 30.000 |
| High resolution limit [Å] | 1.830 |
| Number of reflections | 60986 |
| <I/σ(I)> | 12.2 |
| Completeness [%] | 96.4 |
| Redundancy | 8.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 298 | 35% (v/v) 1,6-hexanediol, 200 mM MgCl2, and 100 mM Tris-Cl buffer, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
