2JET
Crystal structure of a trypsin-like mutant (S189D , A226G) chymotrypsin.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-02-07 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 34.690, 64.351, 44.224 |
| Unit cell angles | 90.00, 102.09, 90.00 |
Refinement procedure
| Resolution | 43.230 - 2.200 |
| R-factor | 0.279 |
| Rwork | 0.276 |
| R-free | 0.33400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kdq |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.824 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 64.420 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.090 | 0.440 |
| Number of reflections | 9753 | |
| <I/σ(I)> | 10.2 | 2.3 |
| Completeness [%] | 98.5 | 95.8 |
| Redundancy | 3.1 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7 | 293 | VAPOR DIFFUSION METHOD, 0.1M HEPES, PH 7.0, 30% PEG6000 AND PROTEIN (15 MG/ML) WITH BENZAMIDINE TWOFOLD EXCESS MIXED 1:1, 20 C |
