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 |
