5BPK
Varying binding modes of inhibitors and structural differences in the binding pockets of different gamma-glutamyltranspeptidases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-26 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.777, 112.006, 91.854 |
| Unit cell angles | 90.00, 90.79, 90.00 |
Refinement procedure
| Resolution | 91.800 - 1.490 |
| R-factor | 0.1449 |
| Rwork | 0.144 |
| R-free | 0.18370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2nqo |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.221 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 91.840 | 1.550 |
| High resolution limit [Å] | 1.490 | 1.490 |
| Rmerge | 0.070 | 0.510 |
| Number of reflections | 176874 | |
| <I/σ(I)> | 16.6 | |
| Completeness [%] | 99.2 | 98.5 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | PEG3350, 0.1M TRIS |
