6KDR
Crystal structure of human NRMT2 in complex with human centromere protein B peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2019-04-07 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97918 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.548, 96.534, 100.213 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.473 - 2.112 |
R-factor | 0.1894 |
Rwork | 0.178 |
R-free | 0.20470 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5cvd |
Data reduction software | DENZO |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX (1.14rc3_3206) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.140 |
High resolution limit [Å] | 2.100 | 5.700 | 2.100 |
Rmerge | 0.120 | 0.054 | 1.361 |
Rmeas | 0.127 | 0.058 | 1.445 |
Rpim | 0.043 | 0.021 | 0.478 |
Total number of observations | 344656 | ||
Number of reflections | 39673 | 2164 | 1953 |
<I/σ(I)> | 9.7 | ||
Completeness [%] | 99.8 | 99.6 | 99.3 |
Redundancy | 8.7 | 7.6 | 8.7 |
CC(1/2) | 0.998 | 0.829 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.3 | 291 | 0.1M Tris pH 8.3, 6% w/v Polyethylene glycol 8000 |