Mass: 18.015 Da / Num. of mol.: 109 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THIS CONSTRUCT (RESIDUES 32-169) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THIS CONSTRUCT (RESIDUES 32-169) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE. LIQUID CHROMATOGRAPHY MASS SPECTROSCOPY (LC/MS) ANALYSIS OF THE PROTEIN PREP PRIOR TO CRYSTALLIZATION SHOWED THAT APPROXIMATELY 1/3 OF THE SAMPLE WAS MISSING AN ADDITIONAL 10 N-TERMINAL AMINO ACID RESIDUES (G-VTGATPKAK) BEYOND THE ENGINEERED TEV CLEAVAGE SITE AND CORRESPONDS TO RESIDUES 41-169 OF THE TARGET SEQUENCE.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 1.96 Å3/Da / Density % sol: 37.24 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5 Details: 2.400000000M (NH4)2SO4, 0.1M Citrate pH 5.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Jun 10, 2010 / Details: Flat mirror (vertical focusing)
Radiation
Monochromator: Single crystal Si(111) bent monochromator (horizontal focusing) Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
0.91837
1
2
0.97917
1
3
0.97874
1
Reflection
Resolution: 1.6→27.264 Å / Num. obs: 16202 / % possible obs: 98.8 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 23.83 Å2 / Rmerge(I) obs: 0.034 / Net I/σ(I): 20.91
Reflection shell
Resolution (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
% possible all
1.6-1.66
0.628
2.5
12098
3193
97.3
1.66-1.72
0.478
3.3
10492
2739
98.6
1.72-1.8
0.312
4.8
12050
3148
98.7
1.8-1.9
0.207
6.9
12374
3229
98.5
1.9-2.02
0.115
11.5
11752
3069
98.9
2.02-2.17
0.074
16.8
11430
2966
99.3
2.17-2.39
0.049
23.7
11852
3089
99.3
2.39-2.73
0.035
32.3
11838
3067
99.6
2.73-3.44
0.023
45.9
11968
3109
99.7
3.44-27.264
0.018
60.6
11783
3089
98.6
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Phasing
Phasing
Method: MAD
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Processing
Software
Name
Version
Classification
NB
SHELX
phasing
REFMAC
5.5.0110
refinement
XSCALE
datascaling
PDB_EXTRACT
3.1
dataextraction
XDS
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 1.6→27.264 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.959 / Occupancy max: 1 / Occupancy min: 0.15 / SU B: 3.629 / SU ML: 0.064 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.088 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE ...Details: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3.ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4.SOLVENT MOLECULES WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 5.SULFATE (SO4) AND GLYCEROL (GOL) FROM THE CRYSTALLIZATION AND CRYOPROTECTANT SOLUTION HAVE BEEN MODELED IN THE SOLVENT STRUCTURE.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.1956
821
5.1 %
RANDOM
Rwork
0.1596
-
-
-
obs
0.1612
16192
98.82 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
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