2ANP
Functional Glutamate 151 to Histidine mutant of the aminopeptidase from Aeromonas Proteolytica.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 2003-12-07 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 109.090, 109.090, 98.417 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 1.900 |
Rwork | 0.180 |
R-free | 0.20500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1AMP with E151 mutated to alanine |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 26278 | |
Completeness [%] | 94.6 | 99.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 298 | 4.5 M NaCL, 100 mM KSCN, 100 mM HEPES, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 25K |