Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX7.2 |
| Synchrotron site | SRS |
| Beamline | PX7.2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-04-08 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.488 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 76.460, 87.930, 124.390 |
| Unit cell angles | 90.00, 106.78, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.800 |
| R-factor | 0.26 |
| Rwork | 0.259 |
| R-free | 0.28000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | THE E.COLI GROES STRUCTURE WITH AMINO ACIDS DIFFERING FROM M.TUBERCULOSIS CHAPERONIN 10 TRUNCATED TO ALANINES |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.400 * |
| Data reduction software | TRUNCATE |
| Data scaling software | XDS |
| Phasing software | DM |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.820 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.050 | 0.611 * |
| Total number of observations | 134674 * | |
| Number of reflections | 38321 | |
| <I/σ(I)> | 24.41 | 1.92 |
| Completeness [%] | 98.0 | 99.7 |
| Redundancy | 3.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.4 | 294 | Roberts, M.M., (1999) Acta Crystallogr.,Sect.D, 55, 910. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | 20 (mM) | ||
| 2 | 1 | reservoir | sodium acetate | 0.1 (M) | |
| 3 | 1 | reservoir | MPD | 30 (%) | pH5.4 |
| 4 | 1 | drop | protein | 20 (mg/ml) |
