4BXF
60S ribosomal protein L27A histidine hydroxylase (MINA53 Y209C) in complex with MN(II), 2-oxoglutarate (2OG) and 60S ribosomal protein L27A (RPL27A G37C) peptide fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-03-16 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 70.340, 88.390, 167.180 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 64.830 - 2.050 |
| R-factor | 0.22 |
| Rwork | 0.220 |
| R-free | 0.22100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4bu2 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.100 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | CNS (1.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 64.830 | 2.160 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.110 | 0.900 |
| Number of reflections | 64784 | |
| <I/σ(I)> | 7 | 2 |
| Completeness [%] | 98.2 | 97.3 |
| Redundancy | 3.3 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | VAPOR DIFFUSION SITTING DROP. 0.1M BIS-TRIS PROPANE PH 8.5, 0.02M NA-K-PHOSPHATE, 20-22% (W/V) PEG 3350, 0.002 M MNCL2, TEMPERATURE 293K |
