5K9T
SecA-N68, a C-terminal truncation of the SecA ATPase from E. coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.105535 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.065, 64.450, 87.967 |
| Unit cell angles | 90.00, 105.85, 90.00 |
Refinement procedure
| Resolution | 17.916 - 2.600 |
| R-factor | 0.2009 |
| Rwork | 0.196 |
| R-free | 0.24970 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3BXZ and 5K94 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.769 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA (3.3.21) |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 84.623 | 40.868 | 2.730 |
| High resolution limit [Å] | 2.590 | 8.200 | 2.590 |
| Rmerge | 0.028 | 0.511 | |
| Number of reflections | 22456 | ||
| <I/σ(I)> | 8.8 | 20 | 1.5 |
| Completeness [%] | 99.4 | 97.8 | 96.8 |
| Redundancy | 4 | 3.9 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 0.1M Tris-HCl pH 8.0, 18% PEG 3000, and 0.9% w/v cadaverine; 18 mg/mL protein concentration. Cryoprotectant included 18% PEG 3000 and 20% PEG 200 |
