4ICQ
Structural basis for substrate recognition and reaction mechanism of bacterial aminopeptidase peps
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 6B |
Synchrotron site | PAL/PLS |
Beamline | 6B |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | BRUKER CCD PROTEUM 300 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 126.644, 126.644, 139.027 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.900 - 2.250 |
R-factor | 0.202 |
Rwork | 0.199 |
R-free | 0.24600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.022 |
RMSD bond angle | 1.874 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | EPMR |
Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.310 |
High resolution limit [Å] | 2.200 | 2.250 |
Number of reflections | 57898 | |
<I/σ(I)> | 46.01 | 5.9 |
Completeness [%] | 99.6 | |
Redundancy | 14.3 | 14.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.6 | 2M MAGNESIUM SULFATE, PH 4.6, MICROBATCH, TEMPERATURE 295K |