2V2B
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E117S- E192A-K248G-R253A-E254A)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | I 4 |
Unit cell lengths | 84.230, 84.230, 91.747 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.350 - 1.500 |
R-factor | 0.167 |
Rwork | 0.166 |
R-free | 0.18400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ojr |
RMSD bond length | 0.010 |
RMSD bond angle | 1.395 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.560 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.040 | 0.320 |
Number of reflections | 44912 | |
<I/σ(I)> | 17.05 | 2.72 |
Completeness [%] | 87.9 | 78.5 |
Redundancy | 3.93 | 2.51 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.5 | 40% (V/V) 1,2-PROPANEDIOL, 50 MM CA ACETATE, 100 MM ACETATE BUFFER (PH 4.5) |