1P8F
A four location model to explain the stereospecificity of proteins.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-02-05 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.00 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 103.306, 103.306, 150.004 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.860 - 1.850 |
R-factor | 0.192 |
Rwork | 0.192 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.014 |
RMSD bond angle | 25.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.073 | 0.473 |
Number of reflections | 69674 | |
<I/σ(I)> | 20.7 | 3.2 |
Completeness [%] | 98.6 | |
Redundancy | 14 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 | 295 | IDH, stored in metal-free final buffer, was diluted to 25, 30, 35 and 40 mg/ml using metal-free 2X buffer; (70mM Na2HPO4 , 18 mM citric acid, 200 mM NaCl, 0.4 mM DTT, pH 5.4). and was crystallized from hanging drops using 5 l each of these IDH solutions and 5 l each of 34, 36, 38, 40, 42, and 44 % (NH4)2SO4 solutions in crystallization buffer (35mM Na2HPO4 , 9 mM citric acid, 100 mM NaCl, 0.2 mM DTT at pH 6.1, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 22K |