3PTL
Crystal structure of proteinase K inhibited by a lactoferrin nonapeptide, Lys-Gly-Glu-Ala-Asp-Ala-Leu-Ser-Leu-Asp at 1.3 A resolution.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2010-05-13 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 68.054, 68.054, 106.750 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 57.380 - 1.300 |
| R-factor | 0.2022 |
| Rwork | 0.200 |
| R-free | 0.24991 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bjr |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.537 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.380 | 1.320 |
| High resolution limit [Å] | 1.300 | 1.300 |
| Number of reflections | 19396 | |
| <I/σ(I)> | 70 | 4 |
| Completeness [%] | 98.2 | 98.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | tris HCl, CaCl2, NaNO3, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
