2V3N
Crystallographic analysis of upper 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 | 2007-04-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 100.830, 100.830, 130.215 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.700 - 2.730 |
| R-factor | 0.213 |
| Rwork | 0.211 |
| R-free | 0.25100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bbc |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.308 |
| 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] | 20.700 | 2.850 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.120 | 0.750 |
| Number of reflections | 21370 | |
| <I/σ(I)> | 9.7 | 1.7 |
| Completeness [%] | 99.3 | 99.9 |
| Redundancy | 3.1 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 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, 15 MM KCN |
