1XMD
M335V mutant structure of mouse carnitine octanoyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-04-27 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9790 |
Spacegroup name | H 3 |
Unit cell lengths | 164.000, 164.000, 159.270 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.000 - 2.100 |
Rwork | 0.196 |
R-free | 0.22400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | COMO |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 92430 | |
Completeness [%] | 99.9 | 99.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 277 | 100mM Hepes, 62% v/v MPD, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 277K |