2C2N
Structure of human mitochondrial malonyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-09-03 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 52.573, 84.828, 74.565 |
Unit cell angles | 90.00, 93.43, 90.00 |
Refinement procedure
Resolution | 74.330 - 1.550 |
R-factor | 0.179 |
Rwork | 0.178 |
R-free | 0.21800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mla |
RMSD bond length | 0.016 |
RMSD bond angle | 1.652 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 52.000 | 1.650 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.080 | 0.280 |
Number of reflections | 94082 | |
<I/σ(I)> | 12.5 | 2.28 |
Completeness [%] | 99.4 | 96.5 |
Redundancy | 4 | 2.44 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 32%PEG4000, 0.25M LI2SO4, 100MM TRIS-HCL, PH8.5, SITTING DROP, 293 K, pH 8.50 |