corrinoid adenosyltransferase / corrinoid adenosyltransferase activity / cobalamin biosynthetic process / ATP binding / metal ion binding Similarity search - Function
Mass: 18.015 Da / Num. of mol.: 141 / Source method: isolated from a natural source / Formula: H2O
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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: 2.2 Å3/Da / Density % sol: 44.06 %
Crystal grow
Temperature: 293 K / Method: batch / pH: 8.5 Details: 0.85 M Ammonium sulfate, 50 mM magnesium chloride, 150 mM sodium chloride, 1.5 mM ATP, 4 mM hydroxocobalamin, pH 8.5, BATCH, temperature 293K
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Data collection
Diffraction
Mean temperature: 100 K
Diffraction source
Source: SYNCHROTRON / Site: APS / Beamline: 19-BM
Detector
Type: SBC-3 / Detector: CCD / Date: Nov 21, 2005
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Relative weight: 1
Reflection
Redundancy: 9.5 % / Av σ(I) over netI: 11.3 / Number: 243527 / Rmerge(I) obs: 0.046 / Χ2: 0.75 / D res high: 1.68 Å / D res low: 50 Å / Num. obs: 25595 / % possible obs: 99.4
Diffraction reflection shell
Highest resolution (Å)
Lowest resolution (Å)
% possible obs (%)
ID
Rmerge(I) obs
Chi squared
Redundancy
1.68
1.74
99.4
1
0.234
0.431
6.8
3.62
50
98.6
1
0.03
0.764
10.8
2.87
3.62
99.5
1
0.041
0.965
11.2
2.51
2.87
99.7
1
0.053
0.892
10.8
2.28
2.51
99.4
1
0.063
0.926
10.6
2.12
2.28
99.5
1
0.075
0.805
10.2
1.99
2.12
99.8
1
0.089
0.686
9.7
1.89
1.99
99.5
1
0.119
0.649
9
1.81
1.89
99.4
1
0.159
0.602
8.3
1.74
1.81
99.7
1
0.206
0.485
7.6
Reflection
Resolution: 1.68→50 Å / Num. obs: 25595 / % possible obs: 99.4 % / Redundancy: 9.5 % / Rmerge(I) obs: 0.046 / Χ2: 0.749 / Net I/σ(I): 11.3
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