1FDY
N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE
Experimental procedure
Source type | ROTATING ANODE |
Source details | MACSCIENCE M18X |
Temperature [K] | 108 |
Detector technology | IMAGE PLATE |
Collection date | 1995-09 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 121.000, 121.000, 196.820 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 6.000 - 2.450 |
R-factor | 0.219 |
Rwork | 0.219 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nal |
RMSD bond length | 0.012 |
RMSD bond angle | 23.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.490 |
High resolution limit [Å] | 2.450 | 2.440 |
Rmerge | 0.041 | 0.245 |
Total number of observations | 148263 * | |
Number of reflections | 60890 | |
<I/σ(I)> | 13.6 | 4.15 |
Completeness [%] | 92.5 | 78 * |
Redundancy | 2.43 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.9 | 37 * | HANGING DROP VAPOR DIFFUSION. WELL: 53% SATURATED AMMONIUM SULFATE, 75 MILLIMOLAR SODIUM PHOSPHATE BUFFER (PH 6.9). DROP: EQUAL VOLUMES OF WELL SOLUTION AND PRE-REACTED ENZYME/HYDROXYPYRUVATE COMPLEX (SEE JRNL REFERENCE), vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium salfate | 53 (%(v/v)sat) | |
2 | 1 | reservoir | sodium phosphate | 75 (mM) | |
3 | 1 | drop | protein | 6.9 (mg/ml) |