2YXE
Crystal structure of L-isoaspartyl protein carboxyl methyltranferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 120 |
Detector technology | CCD |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 60.267, 84.448, 123.091 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.1938 |
Rwork | 0.192 |
R-free | 0.23143 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jg4 |
RMSD bond length | 0.020 |
RMSD bond angle | 1.800 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.037 | |
Number of reflections | 42769 | |
Completeness [%] | 98.1 | 84.5 |
Redundancy | 6.9 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Oil batch | 4.5 | 298 | 0.1M Acetate, 40% 1,2-propanediol, pH 4.5, Oil batch, temperature 298.0K |