2HU5
Binding of inhibitors by Acylaminoacyl-peptidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-05-18 |
Detector | RIGAKU RAXIS IIC |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 63.400, 103.334, 168.224 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.726 - 2.000 |
R-factor | 0.18363 |
Rwork | 0.181 |
R-free | 0.22441 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ve6 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.308 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.726 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.098 | 0.560 |
Number of reflections | 67288 | |
<I/σ(I)> | 15.12 | 2.7 |
Completeness [%] | 89.1 | 53.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 78mM sodium acetate, 0.44mM EDTA, 2.2%PEG 4000, 0.56% beta-octyl-glucoside, 10% DMSO, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |