5F4X
Fructose-1,6-bisphosphate aldolase K229M mutant from rabbit muscle
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-07-18 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9795 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 83.477, 103.194, 84.527 |
Unit cell angles | 90.00, 98.66, 90.00 |
Refinement procedure
Resolution | 35.201 - 1.840 |
R-factor | 0.1464 |
Rwork | 0.146 |
R-free | 0.17390 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1zah |
RMSD bond length | 0.007 |
RMSD bond angle | 1.055 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.201 | 1.910 |
High resolution limit [Å] | 1.840 | 1.840 |
Number of reflections | 122560 | |
<I/σ(I)> | 25.13 | 3.43 |
Completeness [%] | 99.7 | 99.7 |
Redundancy | 3.6 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 296 | Sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K |