1P7V
Structure of a complex formed between Proteinase K and a designed heptapeptide inhibitor Pro-Ala-Pro-Phe-Ala-Ala-Ala at atomic resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-10-11 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.91 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 67.720, 67.720, 101.620 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.080 |
| R-factor | 0.11994 |
| Rwork | 0.120 |
| R-free | 0.13993 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c6 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.411 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.120 |
| High resolution limit [Å] | 1.080 | 1.080 |
| Number of reflections | 101462 | |
| <I/σ(I)> | 28 | 5.61 |
| Completeness [%] | 99.5 | 99 |
| Redundancy | 15.32 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Microgravity with APCF reactors | 6.5 | 295 | tris HCl, CaCl2, NaNO3, pH 6.5, Microgravity with APCF reactors, temperature 295K |
