4ZLA
Bestatin complex structure of leucine aminopeptidase from Helicobacter pylori
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 | 2013-07-27 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.9184 |
Spacegroup name | P 1 |
Unit cell lengths | 99.770, 99.690, 96.780 |
Unit cell angles | 81.89, 60.97, 75.39 |
Refinement procedure
Resolution | 30.552 - 1.900 |
R-factor | 0.178 |
Rwork | 0.176 |
R-free | 0.21940 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3h8g |
RMSD bond length | 0.008 |
RMSD bond angle | 1.018 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.21) |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 96.443 | 30.552 | 2.000 |
High resolution limit [Å] | 1.900 | 6.010 | 1.900 |
Rmerge | 0.027 | 0.302 | |
Rmeas | 0.097 | ||
Rpim | 0.069 | 0.027 | 0.302 |
Total number of observations | 394571 | 11963 | 55259 |
Number of reflections | 230129 | ||
<I/σ(I)> | 7.9 | 19.2 | 2.6 |
Completeness [%] | 92.6 | 84.5 | 90.8 |
Redundancy | 1.7 | 1.8 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 292 | 6% PEG 2K, 50 mM sodium formate, 5.6 mg/ml protein, 1 mM bestatin |