4BAA
Redesign of a Phenylalanine Aminomutase into a beta-Phenylalanine Ammonia Lyase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Collection date | 2011-08-28 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 99.295, 145.837, 99.413 |
Unit cell angles | 90.00, 99.96, 90.00 |
Refinement procedure
Resolution | 48.900 - 2.500 |
R-factor | 0.21072 |
Rwork | 0.209 |
R-free | 0.24637 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2yii |
RMSD bond length | 0.005 |
RMSD bond angle | 0.934 |
Data reduction software | XDS |
Data scaling software | SCALA |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.900 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.120 | 0.380 |
Number of reflections | 94431 | |
<I/σ(I)> | 6.2 | 2.4 |
Completeness [%] | 98.1 | 97.6 |
Redundancy | 2.3 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4 % TACSISMATE, 12 % W/V PEG 3350, 2 MM DTT |