2PBF
Crystal structure of a putative protein-L-isoaspartate O-methyltransferase beta-aspartate methyltransferase (PCMT) from Plasmodium falciparum in complex with S-adenosyl-L-homocysteine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-03-25 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | P 32 |
| Unit cell lengths | 75.156, 75.156, 77.389 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.810 - 2.000 |
| R-factor | 0.22644 |
| Rwork | 0.224 |
| R-free | 0.26789 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1l1n |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.503 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.100 | 0.899 |
| Number of reflections | 33234 | |
| <I/σ(I)> | 22 | 2 |
| Completeness [%] | 99.1 | 90.7 |
| Redundancy | 5.3 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 298 | 25% PEG 3350, 0.2 M (NH4)2SO4, 0.1 M Hepes pH 7.2, 2 mM SAH, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
