2VZK
Structure of the acyl-enzyme complex of an N-terminal nucleophile (Ntn) hydrolase, OAT2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-01-29 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.273, 73.878, 172.166 |
| Unit cell angles | 90.00, 92.71, 90.00 |
Refinement procedure
| Resolution | 171.500 - 2.330 |
| R-factor | 0.25538 |
| Rwork | 0.254 |
| R-free | 0.28432 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vz6 CHAIN A |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.713 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.000 | 2.450 |
| High resolution limit [Å] | 2.330 | 2.330 |
| Rmerge | 0.120 | 0.700 |
| Number of reflections | 62183 | |
| <I/σ(I)> | 6.4 | 2.03 |
| Completeness [%] | 94.2 | 97.9 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 290 | 1.4M AMMONIUM SULPHATE, 100MM N-ACETYL-L-GLUTAMATE, 200MM NACL, 100MM TRIS HCL PH 7.5 |
