6K26
Crystal structure of Vibrio cholerae methionine aminopeptidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2017-06-12 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.542 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.529, 50.010, 131.086 |
Unit cell angles | 90.00, 97.25, 90.00 |
Refinement procedure
Resolution | 34.660 - 1.850 |
R-factor | 0.1679 |
Rwork | 0.166 |
R-free | 0.20760 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2mat |
RMSD bond length | 0.011 |
RMSD bond angle | 1.626 |
Data reduction software | HKL-2000 (v716) |
Data scaling software | HKL-2000 (v716) |
Phasing software | MOLREP (11.6.03) |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 40.000 | 40.000 | 1.920 |
High resolution limit [Å] | 1.850 | 3.980 | 1.850 |
Rmerge | 0.083 | 0.042 | 0.531 |
Rmeas | 0.101 | 0.051 | 0.648 |
Rpim | 0.057 | 0.029 | 0.366 |
Total number of observations | 155933 | ||
Number of reflections | 53682 | 5567 | 5260 |
<I/σ(I)> | 8.9 | ||
Completeness [%] | 98.5 | 98.7 | 97.8 |
Redundancy | 2.9 | 2.9 | 2.8 |
CC(1/2) | 0.997 | 0.618 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 0.1M Hepes, 12 % PEG 3350 |