1T43
Crystal Structure Analysis of E.coli Protein (N5)-Glutamine Methyltransferase (HemK)
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-02-23 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0090,1.0069 |
Spacegroup name | P 63 |
Unit cell lengths | 138.933, 138.933, 40.583 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 3.200 |
R-factor | 0.289 |
Rwork | 0.289 |
R-free | 0.31500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nv8 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.800 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 3.300 |
High resolution limit [Å] | 3.190 | 3.190 |
Rmerge | 0.075 | 0.250 |
Number of reflections | 7675 | |
<I/σ(I)> | 14.8 | 6 |
Completeness [%] | 99.8 | 100 |
Redundancy | 5.1 | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 289 | Ammonium sulfate, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K |