1GTK
Time-resolved and static-ensemble structural chemistry of hydroxymethylbilane synthase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID09 |
Synchrotron site | ESRF |
Beamline | ID09 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1997-06-15 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 87.500, 75.900, 50.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.850 - 1.660 |
R-factor | 0.2 |
Rwork | 0.198 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ypn |
RMSD bond length | 0.021 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | O |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.850 | 1.750 |
High resolution limit [Å] | 1.660 | 1.660 |
Number of reflections | 34417 | |
Completeness [%] | 87.0 | 70.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.3 | PROTEIN WAS CRYSTALLISED AT PH 5.3 IN SITTING DROPS OF 0.05 ML WITH 6-7 MG/ML OF PROTEIN, 0.3 MM EDTA, 15 MM DITHIOTHREITOL, 10%(W/V) PEG6000 AND 0.01% NAN3 IN 0.1 M SODIUM ACETATE. |