3UTL
Human pepsin 3b
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.5 |
Synchrotron site | SRS |
Beamline | PX9.5 |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Collection date | 1994-04-01 |
Detector | MAR scanner 180 mm plate |
Wavelength(s) | 0.92 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.890, 75.270, 87.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 7.970 - 2.610 |
R-factor | 0.13713 |
Rwork | 0.130 |
R-free | 0.19986 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5pep |
RMSD bond length | 0.015 |
RMSD bond angle | 1.795 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 8.000 | 2.780 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.033 | |
Number of reflections | 10426 | |
Completeness [%] | 96.7 | |
Redundancy | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 5.2 | 298 | 16-30 mg/ml protein purified from gastric juice. 30% saturated ammonium sulphate buffered with 200 mM formate, pH 5.2, VAPOR DIFFUSION, temperature 298K |