1Q6H
Crystal structure of a truncated form of FkpA from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2001-11-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97880 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.030, 85.230, 160.740 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.000 - 1.970 |
| R-factor | 0.18383 |
| Rwork | 0.182 |
| R-free | 0.22900 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | FkpA (C-domain 95-226) |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.360 * |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.000 | 2.080 |
| High resolution limit [Å] | 1.970 | 1.970 |
| Rmerge | 0.056 * | 0.206 * |
| Number of reflections | 31307 | 3298 * |
| <I/σ(I)> | 9.7 | 3.4 |
| Completeness [%] | 84.6 | 74.2 |
| Redundancy | 9.9 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 6.5 * | 23 * | PEG 2000, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | Jeffamine M600 | 30 (%(w/v)) | |
| 2 | 1 | reservoir | MES | 0.1 (M) | pH6.5 |
| 3 | 1 | reservoir | 0.05 (M) | ||
| 4 | 1 | drop | protein | 4.4 (mg/ml) |
