Mass: 18.015 Da / Num. of mol.: 359 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH ...THE CONSTRUCT 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
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.33 Å3/Da / Density % sol: 47.16 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6 Details: 0.2000M Ca(OAc)2, 20.0000% PEG-8000, 0.1M MES pH 6.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution: 1.6→27.875 Å / Num. obs: 40560 / % possible obs: 99.9 % / Redundancy: 3.6 % / Biso Wilson estimate: 14.705 Å2 / Rmerge(I) obs: 0.092 / Rsym value: 0.092 / Net I/σ(I): 5.825
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
1.6-1.64
3.6
0.498
1.5
10793
2958
0.498
99.7
1.64-1.69
3.7
0.429
1.7
10489
2873
0.429
99.8
1.69-1.74
3.6
0.346
2.2
10277
2818
0.346
99.9
1.74-1.79
3.6
0.284
2.6
10016
2746
0.284
100
1.79-1.85
3.7
0.237
3.1
9585
2604
0.237
100
1.85-1.91
3.7
0.203
3.7
9407
2566
0.203
100
1.91-1.98
3.7
0.168
4.4
9102
2489
0.168
100
1.98-2.07
3.7
0.132
5.6
8760
2383
0.132
100
2.07-2.16
3.6
0.113
6.5
8443
2315
0.113
100
2.16-2.26
3.7
0.104
7
8024
2182
0.104
100
2.26-2.39
3.7
0.096
7.5
7626
2088
0.096
100
2.39-2.53
3.7
0.087
8
7249
1985
0.087
100
2.53-2.7
3.7
0.086
8
6864
1879
0.086
100
2.7-2.92
3.6
0.074
9.1
6401
1766
0.074
100
2.92-3.2
3.6
0.063
10.2
5810
1613
0.063
100
3.2-3.58
3.6
0.053
10.6
5301
1469
0.053
99.8
3.58-4.13
3.6
0.052
11.4
4686
1316
0.052
99.6
4.13-5.06
3.5
0.057
9.7
3902
1112
0.057
99.5
5.06-7.16
3.4
0.065
9.1
2993
883
0.065
98.9
7.16-27.88
3.1
0.053
10.5
1603
515
0.053
96.4
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Phasing
Phasing
Method: MAD
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Processing
Software
Name
Version
Classification
NB
REFMAC
5.2.0019
refinement
PHENIX
refinement
SHELX
phasing
MolProbity
3beta29
modelbuilding
SCALA
3.2.5
datascaling
PDB_EXTRACT
3.006
dataextraction
MOSFLM
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 1.6→27.875 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.943 / Occupancy max: 1 / Occupancy min: 0.37 / SU B: 2.874 / SU ML: 0.052 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.083 / ESU R Free: 0.084 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 ...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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. (3). ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. (4). ACETATE (ACT) IONS FROM THE CRYSTALLIZATION SOLUTION AND A GLYCEROL (GOL) MOLECULE FROM CRYO SOLUTION WERE MODELED.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.198
2031
5 %
RANDOM
Rwork
0.168
-
-
-
obs
0.169
40506
99.77 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
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