5VTB
Crystal structure of RBBP4 bound to BCL11a peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-04-07 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9786 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.301, 85.264, 87.968 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.320 - 2.400 |
R-factor | 0.203 |
Rwork | 0.201 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4r7a |
RMSD bond length | 0.010 |
RMSD bond angle | 1.080 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | BUSTER (2.10.2) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.440 |
High resolution limit [Å] | 2.390 | 6.510 | 2.400 |
Rmerge | 0.115 | 0.047 | 0.566 |
Rmeas | 0.123 | 0.051 | 0.604 |
Rpim | 0.043 | 0.018 | 0.209 |
Number of reflections | 15853 | ||
<I/σ(I)> | 6.4 | ||
Completeness [%] | 99.7 | 99.3 | 98.7 |
Redundancy | 8.2 | 7.6 | 8 |
CC(1/2) | 0.997 | 0.925 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 25% PEG2000 MME, 0.1 M potassium thiocyanate |