7EHZ
Structure of human NNMT in complex with macrocyclic peptide 2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2018-03-07 |
Detector | RIGAKU RAXIS VII |
Wavelength(s) | 1.54178 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 87.081, 68.057, 45.205 |
Unit cell angles | 90.00, 104.28, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.500 |
R-factor | 0.1966 |
Rwork | 0.193 |
R-free | 0.25520 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3rod |
RMSD bond length | 0.012 |
RMSD bond angle | 1.770 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP (11.6.02) |
Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 5.380 | 2.500 |
Rmerge | 0.066 | 0.044 | 0.274 |
Rmeas | 0.077 | 0.052 | 0.327 |
Rpim | 0.040 | 0.027 | 0.175 |
Number of reflections | 9031 | 931 | 889 |
<I/σ(I)> | 13.9 | ||
Completeness [%] | 99.9 | 99.5 | 100 |
Redundancy | 3.6 | 3.6 | 3.4 |
CC(1/2) | 0.996 | 0.938 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1M Bicine pH9.0, 20% w/v PEG 6000 |