1P2I
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 BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-04-04 |
Detector | MARRESEARCH |
Wavelength(s) | 0.8 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 74.700, 81.000, 124.090 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.410 - 1.650 |
R-factor | 0.201 |
Rwork | 0.201 |
R-free | 0.21000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3btg |
RMSD bond length | 0.004 |
RMSD bond angle | 1.330 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 24.410 | 1.740 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.062 | 0.316 |
Number of reflections | 45488 | |
<I/σ(I)> | 9.7 | 2.4 |
Completeness [%] | 99.8 | 99.9 |
Redundancy | 4.3 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 310 | 50% ammonium sulfate, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 310K |