1V4F
Crystal structures of collagen model peptides with pro-hyp-gly sequence at 1.3A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL40B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL40B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-06-25 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 13.864, 26.181, 19.877 |
| Unit cell angles | 90.00, 105.75, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.260 |
| Rwork | 0.133 |
| R-free | 0.15900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | (PRO-HYP-GLY)10 structure reported in V.Nagarajan S.Kamitori K.Okuyama J.Biochem. 125 310 (1999) |
| RMSD bond length | 0.055 |
| RMSD bond angle | 0.024 |
| Data reduction software | CrystalClear |
| Data scaling software | CrystalClear |
| Phasing software | X-PLOR |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.320 |
| High resolution limit [Å] | 1.260 | 1.260 |
| Rmerge | 0.060 | 0.190 |
| Number of reflections | 3520 | |
| <I/σ(I)> | 3.3 | 3.3 |
| Completeness [%] | 98.0 | 79 |
| Redundancy | 6.67 | 4.66 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | PEG 200, Acetic acid, Sodium azide, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
