1P2N
Structural consequences of accommodation of four non-cognate amino-acid residues in the S1 pocket of bovine trypsin and chymotrypsin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-06-19 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9312 |
Spacegroup name | P 61 |
Unit cell lengths | 100.010, 100.010, 205.100 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 24.000 - 1.800 |
R-factor | 0.199 |
Rwork | 0.199 |
R-free | 0.21300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1cbw |
RMSD bond length | 0.005 |
RMSD bond angle | 1.310 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 24.000 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.061 | 0.180 |
Number of reflections | 104176 | |
<I/σ(I)> | 5.7 | 2.4 |
Completeness [%] | 97.4 | 95.8 |
Redundancy | 2.7 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 295 | 50% ammonium sulfate, 0.1M Tris, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 295K |