Mass: 18.015 Da / Num. of mol.: 921 / 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 THE TARGET SEQUENCE.
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 2.06 Å3/Da / Density % sol: 40.2 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.8 Details: 0.2000M KAcetate, 20.0000% PEG-3350, No Buffer pH 7.8, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Mar 27, 2009 / 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
0.97908
1
Reflection
Resolution: 1.5→29.501 Å / Num. obs: 113854 / % possible obs: 98.5 % / Redundancy: 3.5 % / Biso Wilson estimate: 13.606 Å2 / Rmerge(I) obs: 0.077 / Rsym value: 0.077 / Net I/σ(I): 9.7
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
1.5-1.54
2.5
0.376
2
18029
7300
0.376
86.3
1.54-1.58
2.8
0.331
2.3
21930
7762
0.331
94.7
1.58-1.63
3.5
0.3
2.5
27997
7989
0.3
99.6
1.63-1.68
3.7
0.259
2.9
28546
7792
0.259
100
1.68-1.73
3.7
0.22
3.4
27832
7568
0.22
100
1.73-1.79
3.7
0.181
4.1
26931
7313
0.181
100
1.79-1.86
3.7
0.15
4.7
26084
7064
0.15
100
1.86-1.94
3.7
0.128
5.3
25163
6809
0.128
100
1.94-2.02
3.7
0.108
6
24278
6551
0.108
100
2.02-2.12
3.7
0.094
6.4
23125
6263
0.094
100
2.12-2.24
3.7
0.086
6.6
22114
5967
0.086
100
2.24-2.37
3.7
0.075
7.7
21021
5674
0.075
100
2.37-2.54
3.7
0.07
8.1
19696
5326
0.07
100
2.54-2.74
3.7
0.071
7.3
18324
4956
0.071
100
2.74-3
3.7
0.069
7.3
16888
4590
0.069
100
3-3.35
3.7
0.06
7.8
15338
4170
0.06
100
3.35-3.87
3.7
0.054
9
13555
3713
0.054
100
3.87-4.74
3.6
0.049
9.7
11431
3167
0.049
100
4.74-6.71
3.5
0.048
10.2
8676
2464
0.048
99.8
6.71-29.5
3.3
0.047
10.1
4730
1416
0.047
98.1
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Phasing
Phasing
Method: MAD
-
Processing
Software
Name
Version
Classification
NB
REFMAC
5.5.0053
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: 1.5→29.501 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.966 / Occupancy max: 1 / Occupancy min: 0.3 / SU B: 2.707 / SU ML: 0.045 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.071 / ESU R Free: 0.072 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...Details: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3.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. 4.ACETATE (ACT) AND 1,2-ETHANEDIOL (EDO) FROM THE CRYSTALLIZATION AND CRYOPROTECTANT SOLUTION HAVE BEEN MODELED IN THE SOLVENT STRUCTURE.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.187
5698
5 %
RANDOM
Rwork
0.159
-
-
-
obs
0.16
113785
98.5 %
-
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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