Mass: 63329.492 Da / Num. of mol.: 1 / Fragment: HELICASE DOMAIN, RESIDUES 242-794 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ANAS PLATYRHYNCHOS (mallard) / Plasmid: PFASTBAC / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: D3TI84
Sequence details
ADDITIONAL GAM AT N-TERMINUS AFTER CLEAVAGE OF HIS-TAG
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 2.75 Å3/Da / Density % sol: 55.5 % / Description: NONE
Crystal grow
Details: 12 MG PER ML PROTEIN AND 0.1 M NACL, 0.1M M TRI-SODIUM CITRATE PH 5.6, 12% PEG 4000.
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.976 Å / Relative weight: 1
Reflection
Resolution: 3→50 Å / Num. obs: 13392 / % possible obs: 99.3 % / Observed criterion σ(I): 0 / Redundancy: 3.79 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 16
Reflection shell
Resolution: 3→3.1 Å / Redundancy: 3.81 % / Rmerge(I) obs: 0.71 / Mean I/σ(I) obs: 1.8 / % possible all: 99.8
-
Processing
Software
Name
Version
Classification
REFMAC
5.6.0116
refinement
XDS
datareduction
XSCALE
datascaling
SHELX
phasing
Refinement
Method to determine structure: SAD Starting model: NONE Resolution: 3→33.59 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.901 / SU B: 22.598 / SU ML: 0.41 / Cross valid method: THROUGHOUT / ESU R Free: 0.5 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.29652
646
4.8 %
RANDOM
Rwork
0.21111
-
-
-
obs
0.21511
12746
99.3 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK