2V3P
Crystallographic analysis of beta-axial ligand substitutions in cobalamin bound to transcobalamin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-30 |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 100.390, 100.390, 129.742 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.980 - 2.900 |
| R-factor | 0.196 |
| Rwork | 0.194 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bbc |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.333 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.3.0037) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.300 | 3.060 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.120 | 0.660 |
| Number of reflections | 16711 | |
| <I/σ(I)> | 11.1 | 1.8 |
| Completeness [%] | 97.6 | 99.4 |
| Redundancy | 3.7 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | THE PROTEIN AT 0.5 MM IN 1 M NACL, 0.1 M TRIS, PH 7.5 CRYSTALLIZED FROM 28% PEG 8000, 0.2 M MAGNESIUM ACETATE, 0.1 M TRIS PH 8.5, 20% 2-METHYL-2, 4-PENTADIOL, 40 MM (NH4)2SO3. |
