Mass: 18.015 Da / Num. of mol.: 269 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE CONSTRUCT (RESIDUES 29-279) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 29-279) 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: 2.43 Å3/Da / Density % sol: 49.36 %
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 30.000000000% PEG-400, 0.200000000M LiSO4, 0.1M Cacodylate pH 6.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Jun 9, 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
0.95369
1
2
0.97951
1
3
0.97905
1
Reflection
Resolution: 1.6→28.576 Å / Num. all: 36639 / Num. obs: 36639 / % possible obs: 99.9 % / Redundancy: 3.2 % / Biso Wilson estimate: 16.68 Å2 / Rsym value: 0.079 / Net I/σ(I): 8.5
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
3.1
0.393
1.9
8369
2681
0.393
100
1.64-1.69
3.1
0.348
2.2
8240
2623
0.348
100
1.69-1.74
3.1
0.291
2.6
8052
2565
0.291
100
1.74-1.79
3.1
0.23
3.3
7884
2509
0.23
100
1.79-1.85
3.1
0.197
3.8
7584
2409
0.197
100
1.85-1.91
3.1
0.164
4.3
7359
2337
0.164
100
1.91-1.98
3.2
0.136
5.4
7150
2268
0.136
100
1.98-2.07
3.2
0.117
6
6785
2150
0.117
100
2.07-2.16
3.2
0.101
6.9
6556
2060
0.101
100
2.16-2.26
3.2
0.091
7.5
6430
2025
0.091
100
2.26-2.39
3.2
0.085
7.6
6034
1900
0.085
100
2.39-2.53
3.2
0.086
7.5
5700
1796
0.086
100
2.53-2.7
3.2
0.08
8.1
5348
1673
0.08
100
2.7-2.92
3.2
0.073
8.6
5021
1577
0.073
99.9
2.92-3.2
3.2
0.063
9.6
4600
1441
0.063
99.7
3.2-3.58
3.2
0.056
10.8
4160
1303
0.056
99.7
3.58-4.13
3.2
0.056
10.5
3717
1164
0.056
99.6
4.13-5.06
3.2
0.053
11
3131
978
0.053
99.3
5.06-7.16
3.2
0.059
10.3
2403
757
0.059
99
7.16-28.576
3.1
0.061
9
1313
423
0.061
97.1
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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
SCALA
3.3.15
datascaling
PDB_EXTRACT
3.1
dataextraction
MOSFLM
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 1.6→28.576 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.96 / Occupancy max: 1 / Occupancy min: 0.37 / SU B: 2.724 / SU ML: 0.048 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.076 / ESU R Free: 0.076 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1. 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 ...Details: 1. 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. 2. PEG FRAGMENTS (2PE), SULFATE (SO4) MODELED ARE PRESENT IN CRYSTALLIZATION/CRYO CONDITIONS. 3. DENSITY FOR REGION 143-149 IS POOR AND MODEL IS NOT RELIABLE. 4. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 5. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 6. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.1751
1825
5 %
RANDOM
Rwork
0.1491
-
-
-
obs
0.1504
36638
99.82 %
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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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