#112 - Apr 2009 Oct and Sox Transcription Factors similarity (1)
-
Assembly
Deposited unit
A: Regulation of nuclear pre-mRNA domain-containing protein 1B B: Regulation of nuclear pre-mRNA domain-containing protein 1B C: RPB1-CTD D: Regulation of nuclear pre-mRNA domain-containing protein 1B E: Regulation of nuclear pre-mRNA domain-containing protein 1B F: RPB1-CTD hetero molecules
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.9179 Å / Relative weight: 1
Reflection
Resolution: 1.848→67.353 Å / Num. all: 66812 / Num. obs: 66812 / % possible obs: 99.9 % / Redundancy: 3.8 % / Rsym value: 0.089 / Net I/σ(I): 10.8
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
1.85-1.95
3.8
0.851
0.9
36772
9711
0.851
100
1.95-2.07
3.8
0.467
1.7
35114
9231
0.467
99.9
2.07-2.21
3.8
0.272
2.9
32886
8631
0.272
99.9
2.21-2.39
3.8
0.195
4
30708
8059
0.195
100
2.39-2.62
3.8
0.124
6.2
28228
7418
0.124
100
2.62-2.93
3.8
0.091
8.5
25704
6757
0.091
100
2.93-3.38
3.8
0.059
12.4
22264
5913
0.059
100
3.38-4.14
3.7
0.043
16.2
18559
5030
0.043
100
4.14-5.85
3.7
0.037
17
14336
3896
0.037
100
5.85-44.654
3.6
0.037
14.5
7701
2166
0.037
99.5
-
Phasing
Phasing
Method: molecular replacement
-
Processing
Software
Name
Version
Classification
NB
SCALA
3.3.20
datascaling
MOLREP
phasing
PHENIX
1.8_1069
refinement
PDB_EXTRACT
3.11
dataextraction
XDS
datareduction
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.85→44.654 Å / Occupancy max: 1 / Occupancy min: 0.3 / SU ML: 0.27 / σ(F): 1.01 / Phase error: 30.77 / Stereochemistry target values: ML Details: xprep was used for the analysis of diffraction intensities. refmac, autobuster, molrep, coot, the molprobity server were also used during refinement. Some uninterpreted electron density ...Details: xprep was used for the analysis of diffraction intensities. refmac, autobuster, molrep, coot, the molprobity server were also used during refinement. Some uninterpreted electron density likely represents additional N-terminal residues of the CID construct, but fails to resolve a continuous trace of the protein chain. scaling of diffraction data in a c-centered orthorhombic setting with cell dimensions a, b, c = 66.5, 89.3, 134.8 Angstroms produced reasonable merging statistics, but model refinement progressed poorly in that setting. The L-test as implemented by PHENIX.XTRIAGE detected intensity statistics suggestive of twinning. Twin refinement was not pursued due to diminished map interpretability and poor comparability of R-factors, caveats cited in the PHENIX.XTRIAGE program output. We thank Huanwang Yang for helpful discussion.
Rfactor
Num. reflection
% reflection
Rfree
0.2709
2024
3.03 %
Rwork
0.2378
64737
-
obs
0.2389
66761
99.92 %
Solvent computation
Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
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