Mass: 18.015 Da / Num. of mol.: 88 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH ...THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 1-188 OF THE TARGET SEQUENCE.
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Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.96 Å3/Da / Density % sol: 58.39 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 4.2 Details: 0.4M KH2PO4, 1.6M NaH2PO4, 0.1M Phosphate Citrate pH 4.2, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 22, 2013 Details: Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (horizontal focusing)
Radiation
Monochromator: single crystal Si(111) bent / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
0.97917
1
2
0.91837
1
3
0.97845
1
Reflection
Resolution: 2.5→26.002 Å / Num. all: 17497 / Num. obs: 17497 / % possible obs: 98.4 % / Redundancy: 3.6 % / Rsym value: 0.106 / Net I/σ(I): 9
Reflection shell
Diffraction-ID: 1
Resolution (Å)
Redundancy (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
2.5-2.57
3.6
0.85
1.6
4683
1300
0.85
99
2.57-2.64
3.6
0.66
2
4547
1265
0.66
99.4
2.64-2.71
3.5
0.545
2.4
4177
1201
0.545
98.3
2.71-2.8
3
0.465
2.6
3584
1191
0.465
97.1
2.8-2.89
3.4
0.348
3.5
3980
1171
0.348
98.6
2.89-2.99
3.8
0.292
4.4
4230
1104
0.292
99.6
2.99-3.1
3.8
0.235
5.4
4108
1091
0.235
99.7
3.1-3.23
3.8
0.194
6.4
3975
1059
0.194
99.2
3.23-3.37
3.7
0.147
7.9
3645
982
0.147
98.7
3.37-3.54
3.7
0.096
11.2
3532
955
0.096
98.6
3.54-3.73
3.6
0.088
12.2
3250
902
0.088
98.4
3.73-3.95
3.3
0.075
13.3
2761
833
0.075
96.6
3.95-4.23
3
0.058
14.7
2291
767
0.058
94.4
4.23-4.56
3.8
0.049
20.5
2925
768
0.049
99.4
4.56-5
3.8
0.051
19.4
2620
693
0.051
99.7
5-5.59
3.8
0.057
18.3
2416
638
0.057
99.6
5.59-6.46
3.5
0.065
15.3
1953
559
0.065
98
6.46-7.91
3.2
0.061
17
1431
453
0.061
95
7.91-11.18
3.7
0.039
28
1374
367
0.039
98.5
11.18-26.002
3.9
0.04
29.1
776
198
0.04
92.1
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Phasing
Phasing
Method: MAD
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Processing
Software
Name
Version
Classification
NB
MolProbity
3beta29
modelbuilding
PDB_EXTRACT
3.1
dataextraction
SOLVE
phasing
SCALA
3.3.20
datascaling
BUSTER-TNT
2.10.0
refinement
MOSFLM
datareduction
BUSTER
2.10.0
refinement
Refinement
Method to determine structure: MAD / Resolution: 2.5→26.002 Å / Cor.coef. Fo:Fc: 0.9246 / Cor.coef. Fo:Fc free: 0.8967 / Occupancy max: 1 / Occupancy min: 0.5 / Cross valid method: THROUGHOUT / σ(F): 0 Details: 1. ZERO OCCUPANCY HYDROGENS WERE INCLUDED DURING REFINEMENT TO IMPROVE THE ANTI-BUMPING RESTRAINTS. 2. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORDS CONTAIN SUM OF ...Details: 1. ZERO OCCUPANCY HYDROGENS WERE INCLUDED DURING REFINEMENT TO IMPROVE THE ANTI-BUMPING RESTRAINTS. 2. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORDS CONTAIN SUM OF TLS AND RESIDUAL U FACTORS. 3. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 4. 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. 5. CHLORIDE (CL) AND PHOSPHATE (PO4) MOLECULE FROM THE PURIFICATION AND CRYSTALLIZATION SOLUTION ARE MODELED. 6. NCS RESTRAINTS WERE APPLIED DURING REFINEMENT USING LSSR (-AUTONCS) IN BUSTER. 7. MAD PHASE RESTRAINTS WERE USED DURING REFINEMENT.
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