5FJO
N-acyl amino acid racemase from Amycolatopsis sp. Ts-1-60: G291D- F323Y mutant in complex with N-acetyl naphthylalanine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04-1 |
Synchrotron site | Diamond |
Beamline | I04-1 |
Temperature [K] | 120 |
Collection date | 2013-12-13 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 164.710, 164.710, 169.590 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 68.550 - 2.080 |
R-factor | 0.14606 |
Rwork | 0.145 |
R-free | 0.17465 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4a6g |
RMSD bond length | 0.020 |
RMSD bond angle | 1.992 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 68.550 | 2.130 |
High resolution limit [Å] | 2.080 | 2.080 |
Rmerge | 0.160 | 0.740 |
Number of reflections | 69708 | |
<I/σ(I)> | 15.5 | 4.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 13.5 | 14.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 100 MM TRIS HCL PH 8.0, 15% PEG 4K, 800 MM SODIUM FORMATE, PROTEIN AT 8 MG PER ML |