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 |