2B9E
Human NSUN5 protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-10-04 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 56.289, 56.289, 178.666 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 59.550 - 1.650 |
R-factor | 0.18807 |
Rwork | 0.186 |
R-free | 0.22226 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ixk |
RMSD bond length | 0.010 |
RMSD bond angle | 1.326 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 59.550 | 1.693 |
High resolution limit [Å] | 1.650 | 1.650 |
Number of reflections | 38415 | |
Completeness [%] | 99.8 | 90 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 300 | NSUN5 was complexed with S-adenosyl-L-methionine (SAM) (Sigma) at 1:10 molar ratio of protein :SAM and crystallized using the sitting drop vapor diffusion method at 20 C by mixing 1 l of the protein solution with 1 l of the reservoir solution containing 10% Iso-propanole, 20% PEG 4000, 0.1M Na HEPES pH 7.5. , VAPOR DIFFUSION, HANGING DROP, temperature 300K |