2WPB
Crystal structure of the E192N mutant of E. Coli N-acetylneuraminic acid lyase in complex with pyruvate and the inhibitor (2R,3R)-2,3,4- trihydroxy-N,N-dipropylbutanamide in space group P21 crystal form I
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-05-13 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 57.020, 143.741, 84.304 |
| Unit cell angles | 90.00, 109.90, 90.00 |
Refinement procedure
| Resolution | 71.880 - 2.050 |
| R-factor | 0.19176 |
| Rwork | 0.190 |
| R-free | 0.23394 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wnn |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.283 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.5.0097) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 79.310 | 2.160 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.090 | 0.440 |
| Number of reflections | 78597 | |
| <I/σ(I)> | 8.6 | 2.6 |
| Completeness [%] | 98.6 | 96.3 |
| Redundancy | 3.5 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.2 | 100MM TRIS-HCL PH 8.2, 200 MM NACL, 18% PEG 3350 |
