1UMU
STRUCTURE DETERMINATION OF UMUD' BY MAD PHASING OF THE SELENOMETHIONYL PROTEIN
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-08 |
| Detector | FUJI |
| Wavelength(s) | 0.9871, 0.9794, 0.9792, 0.9686; 0.9793, 0.9791, 0.9686 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 52.800, 52.800, 160.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.500 |
| R-factor | 0.207 |
| Rwork | 0.207 |
| R-free | 0.30300 |
| Structure solution method | MAD METHOD |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.800 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 (MODIFIED LOCALLY) |
| Phasing software | MADSYS |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.100 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.067 | |
| Number of reflections | 7500 | |
| <I/σ(I)> | 2 | |
| Completeness [%] | 98.0 | |
| Redundancy | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.8 | 20 * | THE CRYSTALS WERE GROWN FROM 600MM LISO4, 20MM MGCL2, 100MM CACODYLATE BUFFER PH 5.8, 5MM DTT AT 20C WITH A PROTEIN CONCENTRATION OF 12-15 MG/ML. THE CRYSTALS WERE FROZEN AT 100K IN PARATONE FOR DATA COLLECTION AT THE NSLS X4A BEAMLINE. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | cacodylate | 100 (mM) | |
| 2 | 1 | reservoir | 600 (mM) | ||
| 3 | 1 | reservoir | 20 (mM) | ||
| 4 | 1 | reservoir | DTT | 5 (mM) | |
| 5 | 1 | reservoir | free DL-methionine | 2 (mg/ml) |
