1KQ5
C-terminal Domain of Cyclase Associated Protein with PRO 505 Replaced by SER (P505S)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X9B |
| Synchrotron site | NSLS |
| Beamline | X9B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-11-21 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.04 |
| Spacegroup name | I 21 21 21 |
| Unit cell lengths | 56.370, 86.610, 160.440 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 3.000 |
| R-factor | 0.237 |
| Rwork | 0.230 |
| R-free | 0.26800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k4z |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.310 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 3.190 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.058 | 0.097 |
| Number of reflections | 7755 | |
| <I/σ(I)> | 34.6 | 12.2 |
| Completeness [%] | 97.5 | 93.2 |
| Redundancy | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | PEG 4000, lithium sulfate, hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
