1LLQ
Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-02-05 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.947 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 130.620, 130.620, 149.230 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 * - 2.300 |
R-factor | 0.247 * |
Rwork | 0.247 |
R-free | 0.28000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qr6 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.249 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.370 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.047 | 0.224 |
Total number of observations | 308683 * | |
Number of reflections | 62146 * | |
<I/σ(I)> | 30 | 6.3 |
Completeness [%] | 94.6 * | 99.3 |
Redundancy | 4.7 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | Clancy, L.L., (1992) J. Mol. Biol., 226, 565. * |