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 |