3EBG
Structure of the M1 Alanylaminopeptidase from malaria
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ELLIOTT GX-13 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-10-20 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 75.656, 108.684, 118.399 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.600 - 2.100 |
R-factor | 0.17279 |
Rwork | 0.170 |
R-free | 0.22034 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.134 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.600 | 2.210 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.071 | 0.340 |
Number of reflections | 53946 | |
<I/σ(I)> | 2.3 | |
Completeness [%] | 95.5 | 82.3 |
Redundancy | 2.7 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 22% (v/v) PEG 8000, 10% (v/v) glycerol, 0.1 M Tris (pH 8.5), 0.2 M MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |