1THF
CYCLASE SUBUNIT OF IMIDAZOLEGLYCEROLPHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-12-15 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9789, 0.9795, 0.98085 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 79.680, 44.420, 63.910 |
Unit cell angles | 90.00, 112.01, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.450 |
R-factor | 0.198 |
Rwork | 0.178 |
R-free | 0.21400 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.020 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.000 | 1.440 |
High resolution limit [Å] | 1.420 * | 1.420 * |
Rmerge | 0.056 * | 0.113 * |
Number of reflections | 37314 * | |
<I/σ(I)> | 20.6 | 7.3 |
Completeness [%] | 95.1 * | 94.6 |
Redundancy | 6.0 * | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.8 | 20 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 24.6 (mg/ml) |