2WJZ
Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM16 |
| Synchrotron site | ESRF |
| Beamline | BM16 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-12 |
| Detector | ADSC CCD |
| Spacegroup name | P 32 |
| Unit cell lengths | 93.935, 93.935, 166.330 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.511 - 2.601 |
| R-factor | 0.1869 |
| Rwork | 0.185 |
| R-free | 0.21840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gpw |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.993 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 81.350 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.070 | 0.420 |
| Number of reflections | 50263 | |
| <I/σ(I)> | 21.5 | 4.43 |
| Completeness [%] | 99.6 | 99.7 |
| Redundancy | 3.9 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | PEG8K 10-12%, 100 MM HEPES PH = 8.5 22.5MM NH4NO3 / NH4AC 5% (V/V) MPD 10 MM DTT 20 MM L-GLN PROT. CONC.= 12 MG/ML |
