5UJC
Crystal structure of a C.elegans B12-trafficking protein CblC, a human MMACHC homologue
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-22 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.03325 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.008, 66.089, 92.826 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 53.840 - 1.350 |
| R-factor | 0.13361 |
| Rwork | 0.132 |
| R-free | 0.16303 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3sbz |
| RMSD bond length | 0.015 |
| RMSD bond angle | 2.013 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.840 | 1.370 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.054 | 0.573 |
| Rpim | 0.029 | 0.435 |
| Number of reflections | 66799 | 2029 |
| <I/σ(I)> | 15 | 1.9 |
| Completeness [%] | 92.9 | 58.7 |
| Redundancy | 3.8 | 2.3 |
| CC(1/2) | 0.997 | 0.618 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 21.5% PEG 3350, 40 mM Spermidine-HCl, 0.2 M (NH4)2tartarate |
