5E1M
Crystal structure of NTMT1 in complex with PPKRIA peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-06-22 |
Detector | RIGAKU SATURN A200 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 107.406, 107.406, 205.604 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.680 - 1.750 |
R-factor | 0.1621 |
Rwork | 0.161 |
R-free | 0.18820 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | isomorphous crystal structure of same protein. |
RMSD bond length | 0.017 |
RMSD bond angle | 1.758 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.9) |
Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 29.680 | 29.680 | 1.780 |
High resolution limit [Å] | 1.750 | 9.090 | 1.750 |
Rmerge | 0.108 | 0.031 | 0.942 |
Rmeas | 0.111 | 0.032 | 0.966 |
Rpim | 0.024 | 0.008 | 0.210 |
Total number of observations | 1466692 | 9256 | 78475 |
Number of reflections | 71201 | ||
<I/σ(I)> | 27 | 82.7 | 4.3 |
Completeness [%] | 100.0 | 97.2 | 99.9 |
Redundancy | 20.6 | 15 | 20.4 |
CC(1/2) | 0.999 | 1.000 | 0.910 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | 26% PEG3350, 16% tacsimate |