1HL2
Crystal structure of N-acetylneuraminate lyase from E. coli mutant L142R in complex with b-hydroxypyruvate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Collection date | 2002-09-15 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 83.740, 95.990, 89.650 |
| Unit cell angles | 90.00, 115.16, 90.00 |
Refinement procedure
| Resolution | 37.400 - 1.800 |
| R-factor | 0.183 |
| Rwork | 0.183 |
| R-free | 0.21000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fdy |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.500 |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.400 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.071 | 0.300 |
| Total number of observations | 412908 * | |
| Number of reflections | 117329 | |
| <I/σ(I)> | 5.2 | 2.4 |
| Completeness [%] | 98.8 | 97.7 |
| Redundancy | 3.5 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.6 * | 21 * | pH 4.60 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | drop | BHP | 20 (mM) | |
| 3 | 1 | drop | Tris | 20 (mM) | pH7.6 |
| 4 | 1 | reservoir | sodium acetate | 100 (mM) | pH4.6 |
| 5 | 1 | reservoir | PEG4000 | 8 (%(w/v)) |
