1BV4
APO-MANNOSE-BINDING PROTEIN-C
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-05-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 32.390, 132.620, 46.810 |
| Unit cell angles | 90.00, 94.28, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.850 |
| R-factor | 0.212 |
| Rwork | 0.212 |
| R-free | 0.25600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1rdo |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.400 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | CNS (0.3C) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.039 | 0.260 |
| Number of reflections | 33667 | |
| <I/σ(I)> | 20.6 | 6.2 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 3.7 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | 12% PEG 8000, 100 MM NAMES, PH 6.1, 200 MM LICL, 2 MM EDTA 0.02%, NAN3, pH 6.2 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | reservoir | PEG8000 | 8-12 (%(w/v)) | |
| 3 | 1 | reservoir | Tris-Cl | 100 (mM) | pH8.0 |
| 4 | 1 | reservoir | 10 (mM) | ||
| 5 | 1 | reservoir | 0.02 (%) | ||
| 6 | 1 | reservoir | 0.375 (mM) |
