3ZLF
Structure of group A Streptococcal enolase K312A mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-03-31 |
| Detector | ADSC QUANTUM 210r |
| Spacegroup name | P 4 |
| Unit cell lengths | 181.620, 181.620, 56.413 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 90.810 - 2.150 |
| R-factor | 0.1763 |
| Rwork | 0.172 |
| R-free | 0.19910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w6t |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.866 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.810 | 2.230 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.240 | 1.210 |
| Number of reflections | 100879 | |
| <I/σ(I)> | 10.64 | 2.13 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 11.8 | 10.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 1-3.5 M SODIUM/POTASSIUM PHOSPHATE BUFFER (PH 5-7.5), 2% PEG 400 |






