1KR5
Crystal structure of human L-isoaspartyl methyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X8C |
Synchrotron site | NSLS |
Beamline | X8C |
Temperature [K] | 118 |
Detector technology | CCD |
Collection date | 2001-03-08 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.100 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 48.007, 53.698, 49.003 |
Unit cell angles | 90.00, 115.60, 90.00 |
Refinement procedure
Resolution | 44.190 - 2.100 |
R-factor | 0.221 * |
Rwork | 0.221 |
R-free | 0.26400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jg1 |
RMSD bond length | 0.007 |
RMSD bond angle | 23.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.200 * | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.074 | 0.256 |
Total number of observations | 47131 * | |
Number of reflections | 12501 | |
Completeness [%] | 94.7 | 75 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 6.5 | 293 | PEG 8000, Magnesium acetate, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | 0.2 (M) | ||
2 | 1 | 1 | cacodylate | 0.1 (M) | pH6.5 |
3 | 1 | 1 | PEG8000 | 20 (%) |