1V6Q
Crystal Structures of Collagen Model Peptides with Pro-Hyp-Gly Sequence at 1.3 A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL40B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL40B2 |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2002-06-25 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 14.051, 26.775, 20.004 |
| Unit cell angles | 90.00, 106.76, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.250 |
| Rwork | 0.135 |
| R-free | 0.18860 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | (Pro-Hyp-Gly)10 structure reported in V.Nagarajan S.Kamitori and K.Okuyama J.Biochem. 125 310 (1999). |
| RMSD bond length | 0.018 |
| RMSD bond angle | 0.023 |
| Data reduction software | CrystalClear |
| Data scaling software | CrystalClear |
| Phasing software | SHELX |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.150 | 1.300 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmerge | 0.057 | 0.235 |
| Number of reflections | 3768 | |
| <I/σ(I)> | 7.6 | 2.4 |
| Completeness [%] | 94.5 | 67.7 |
| Redundancy | 3.4 |
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 |
