3EBH
Structure of the M1 Alanylaminopeptidase from malaria complexed with bestatin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-03-15 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 75.651, 108.628, 117.964 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.470 - 1.650 |
R-factor | 0.1783 |
Rwork | 0.177 |
R-free | 0.20219 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 0.973 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.2.21) |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 27.570 | 46.520 | 1.740 |
High resolution limit [Å] | 1.650 | 5.220 | 1.650 |
Rmerge | 0.064 | 0.039 | 0.369 |
Number of reflections | 120212 | ||
<I/σ(I)> | 8.673 | 14.8 | 1.8 |
Completeness [%] | 83.2 | 98 | 74.6 |
Redundancy | 2.8 | 3.5 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | vapor diffusion, hanging dro | 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 dro, temperature 298K |