3V49
Structure of ar lbd with activator peptide and sarm inhibitor 1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-12-12 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.629, 67.331, 69.809 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.000 - 1.700 |
R-factor | 0.185 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 2ama |
RMSD bond length | 0.011 |
RMSD bond angle | 0.033 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELX |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.900 | 1.800 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.043 | 0.185 |
Number of reflections | 28211 | |
<I/σ(I)> | 29.6 | 6.5 |
Completeness [%] | 98.3 | 97.6 |
Redundancy | 4.5 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 291 | Hanging drop set up as a 50:50 mixture of 1 microL protein+1 microL reservoir with: A) protein solution = 80 microL hAR LBD (3.5 mg/ml) + 1.5 microL activator undecapeptide (GAFQNLFQSVR)+1 microL LiSO4 (0.2 M) in HEPES buffer 0.1 M + 0.5 mg inhibitor 1 (PK0) B) Reservoir = 1 ml HEPES buffer 0.1 M + PEG 4000 12-20 %, pH 7.5, VAPOR DIFFUSION, temperature 291K | |
1 | 7.5 | 291 | Hanging drop set up as a 50:50 mixture of 1 microL protein+1 microL reservoir with: A) protein solution = 80 microL hAR LBD (3.5 mg/ml) + 1.5 microL activator undecapeptide (GAFQNLFQSVR)+1 microL LiSO4 (0.2 M) in HEPES buffer 0.1 M + 0.5 mg inhibitor 1 (PK0) B) Reservoir = 1 ml HEPES buffer 0.1 M + PEG 4000 12-20 %, pH 7.5, VAPOR DIFFUSION, temperature 291K |