5LKX

Crystal structure of the p300 acetyltransferase catalytic core with propionyl-coenzyme A.


X-RAY DIFFRACTION Experimental Data & Validation


X-ray Experimental Help

Crystallization

Crystalization Experiments
Method Vapor Diffusion Sitting Drop
Temperature 277.0
Details Tris, PEG MME 2000, DMSO

Crystal Data

Unit Cell
Length (Å) Angle (°)
a = 93.81 α = 90
b = 155.26 β = 90
c = 109.79 γ = 90
Symmetry
Space Group C 2 2 21

Diffraction

Diffraction Experiment
ID # Data Collection Temperature
1 100
Diffraction Detector
Detector Diffraction Type Details Collection Date
PIXEL DECTRIS PILATUS3 2M -- 2015-11-28
Diffraction Radiation
Monochromator Protocol
-- SINGLE WAVELENGTH
Diffraction Detector Source
Source Type Wavelength List Synchrotron Site Beamline
SYNCHROTRON ESRF BEAMLINE ID23-2 0.872600 ESRF ID23-2

Data Collection

Overall
Resolution (High) Resolution (Low) Percent Possible (Observed) R Merge I (Observed) R Sym I (Observed) Net I Over Average Sigma (I) Redundancy Number Reflections (All) Number Reflections (Observed) Observed Criterion Sigma (F) Observed Criterion Sigma (I) B (Isotropic) From Wilson Plot
2.52 30 99.5 -- -- -- 5.2 -- 27348 -- -- --
High Resolution Shell
Resolution (High) Resolution (Low) Percent Possible (All) R Merge I (Observed) R-Sym I (Observed) Mean I Over Sigma (Observed) Redundancy Number Unique Reflections (All)
2.52 2.54 98.3 -- -- 1.48 5.3 --

Refinement

Statistics
Structure Solution Method Refinement High Resolution Refinement Low Resolution Cut-off Sigma (I) Cut-off Sigma (F) Number of Reflections (All) Number of Reflections (Observed) Number of Reflections (R-Free) Percent Reflections (Observed) R-Factor (All) R-Factor (Observed) R-Work R-Free R-Free Selection Details
MOLECULAR REPLACEMENT 2.52 30.0 -- -- -- 25997 1351 99.59 -- 0.20828 0.20671 0.23944 RANDOM
High Resolution Shell
Refinement method Shell Resolution (High) Shell Resolution (Low) # of Reflections (Observed) # of Reflections (R-Free) # of Reflections (R-Work) R-Factor (R-Work) R-Factor (R-Free) R-Factor (R-Free Error) Percent Reflections (Observed)
X Ray Diffraction 2.52 2.585 -- 91 1901 0.33 0.377 -- 99.4
Temperature Factor Modeling
Temperature Factor Value
Mean Isotropic B 55.942
Anisotropic B[1][1] 3.09
Anisotropic B[1][2] 0.0
Anisotropic B[1][3] 0.0
Anisotropic B[2][2] 0.0
Anisotropic B[2][3] 0.0
Anisotropic B[3][3] -3.09
RMS Deviations
Key Refinement Restraint Deviation
r_mcangle_other 5.902
r_angle_other_deg 1.028
r_long_range_B_refined 10.771
r_scbond_other 3.956
r_mcangle_it 5.903
r_dihedral_angle_3_deg 12.912
r_dihedral_angle_1_deg 5.737
r_gen_planes_other 0.002
r_bond_other_d 0.004
r_dihedral_angle_2_deg 34.045
r_angle_refined_deg 1.321
r_scbond_it 3.956
r_long_range_B_other 10.768
r_mcbond_other 3.629
r_gen_planes_refined 0.007
r_chiral_restr 0.068
r_scangle_other 6.426
r_bond_refined_d 0.011
r_dihedral_angle_4_deg 16.216
r_mcbond_it 3.629
Number of Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms Numbers
Protein Atoms 4496
Nucleic Acid Atoms 0
Heterogen Atoms 72
Solvent Atoms 171

Software

Software
Software Name Purpose
REFMAC refinement version: 5.8.0135
XDS data reduction
XSCALE data scaling
PHASER phasing