5KBY
Crystal structure of dipeptidyl peptidase IV in complex with SYR-472
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-11 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.987 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 121.573, 122.165, 143.704 |
| Unit cell angles | 90.00, 114.57, 90.00 |
Refinement procedure
| Resolution | 34.570 - 2.240 |
| R-factor | 0.1764 |
| Rwork | 0.174 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3g0b |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.246 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0025) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.300 |
| High resolution limit [Å] | 2.250 | 5.550 | 2.250 |
| Rmerge | 0.083 | 0.031 | 0.541 |
| Total number of observations | 712558 | ||
| Number of reflections | 178650 | ||
| <I/σ(I)> | 9.5 | ||
| Completeness [%] | 98.9 | 99.9 | 88.8 |
| Redundancy | 4 | 4.2 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 22.2% PEG MME 2000, 0.1M Bicine pH 8.5 |
