Mass: 18.015 Da / Num. of mol.: 191 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THIS CONSTRUCT (RESIDUES 30-288) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THIS CONSTRUCT (RESIDUES 30-288) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY 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: 4.02 Å3/Da / Density % sol: 69.43 % Description: THE STATISTICS REPORTED IN REMARK 200 WERE COMPUTED WITH XSCALE WITH FRIEDEL PAIRS KEPT SEPARATE.
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 9.1 Details: 0.200M Na2HPO4, 20.00% PEG-3350, No Buffer, pH 9.1, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
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
0.97931
1
3
0.97868
1
Reflection
Resolution: 2.4→28.825 Å / Num. obs: 18955 / % possible obs: 98.1 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 40.298 Å2 / Rmerge(I) obs: 0.195 / Net I/σ(I): 6.88
Reflection shell
Resolution (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
% possible all
2.4-2.49
0.979
1.5
13833
3524
94
2.49-2.58
0.846
1.8
12555
3200
98.5
2.58-2.7
0.674
2.2
14339
3645
98.1
2.7-2.84
0.548
2.8
13590
3462
98.6
2.84-3.02
0.419
3.6
14129
3598
98.5
3.02-3.25
0.261
5.6
13706
3488
98.3
3.25-3.58
0.165
8.5
14249
3620
98.8
3.58-4.09
0.103
12.6
13749
3503
98.8
4.09-5.14
0.086
14.6
14077
3579
99
5.14-28.825
0.084
15
14209
3616
98.2
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Phasing
Phasing
Method: MAD
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Processing
Software
Name
Version
Classification
NB
SHELX
phasing
REFMAC
5.5.0102
refinement
XSCALE
datascaling
PDB_EXTRACT
3.1
dataextraction
XDS
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 2.4→28.825 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.932 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 11.169 / SU ML: 0.142 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.191 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4. WATERS WERE ...Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 5. 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. 7. POLYETHYLENE GLYCOL-3350 (PEG) FRAGMENTS AND ETHYLENE GLYCOL (EDO) FROM THE CRYSTALLIZATION/CRYOPROTECTION SOLUTION AND A SODIUM ION (NA) FROM THE PROTEIN BUFFER ARE MODELED.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.2166
965
5.1 %
RANDOM
Rwork
0.1694
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-
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obs
0.1718
18936
98.26 %
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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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