1Y1N
Identification of SH3 motif in M. Tuberculosis methionine aminopeptidase suggests a mode of interaction with the ribosome
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9770 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.335, 47.908, 56.819 |
Unit cell angles | 90.00, 95.11, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.510 |
R-factor | 0.213 |
Rwork | 0.202 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1c21 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.401 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.560 |
High resolution limit [Å] | 1.510 | 1.510 |
Rmerge | 0.046 | 0.164 |
Number of reflections | 41440 | |
<I/σ(I)> | 30.6 | 7.67 |
Completeness [%] | 99.5 | 97.1 |
Redundancy | 26 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.5 | 273 | Bistris, PEG monomethyl ether 2000, KCl, HEPES, NaCl, pH 6.5, VAPOR DIFFUSION, temperature 273K |