2E0X
Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli (monoclinic form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-29 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.230, 127.900, 75.140 |
| Unit cell angles | 90.00, 94.78, 90.00 |
Refinement procedure
| Resolution | 29.910 - 1.950 |
| R-factor | 0.195 |
| Rwork | 0.193 |
| R-free | 0.23100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | A MOLECULE (CHAIN ID A B) OF THE PDB ENTRY 2DBU |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.256 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.095 | 0.317 |
| Number of reflections | 89113 | |
| <I/σ(I)> | 9.2 | |
| Completeness [%] | 98.2 | 96.4 |
| Redundancy | 3.2 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 277 | 20% PEG 4000, 0.2M calcium chloride, 0.1M Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
