3L6R
The structure of mammalian serine racemase: Evidence for conformational changes upon inhibitor binding
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-03 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.98000 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 54.543, 84.212, 70.376 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.780 - 1.700 |
Rwork | 0.168 |
R-free | 0.20200 |
Structure solution method | SAD |
RMSD bond length | 0.030 |
RMSD bond angle | 2.064 |
Data reduction software | d*TREK |
Data scaling software | d*TREK |
Phasing software | SHELXS |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.780 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.094 | 0.280 |
Number of reflections | 35305 | |
<I/σ(I)> | 16.1 | 4.5 |
Completeness [%] | 97.1 | 78.9 |
Redundancy | 12.45 | 5.44 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 295 | PEG 3350, 200mM sodium malonate, 50mM MnCl2, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 295K |