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| Title: | | RNA POLYMERASE II STRAND SEPARATED ELONGATION COMPLEX, MISMATCHED NUCLEOTIDE | |
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| Molecular Description: |
DNA-directed RNA polymerase II largest subunit (E.C.2.7.7.6)/DNA-directed RNA polymerase II 140 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerase II 45 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 27 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 23 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 14.5 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerase II 14.2 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 8.3 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerase II 13.6 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 7.7 kDa polypeptide (E.C.2.7.7.6)/DNA/RNA Complex |
 |
| Structural Features: | DOUBLE HELIX |
|
| Nucleic Acid Sequence: |
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|
| Protein Sequence: |
|
|
| Primary Citation: | Westover, K.D., Bushnell, D.A., Kornberg, R.D.
Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center.
Cell(Cambridge,Mass.)
, 119,
pp. 481 - 489, 2004.
|
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| | | |
| Experimental Information: | X-RAY DIFFRACTION |
|
| Space Group: |
C
1
2
1
|
|
| Cell Constants: |
| a = 168.846 | b = 222.958 | c = 193.602 | (Ångstroms) |
 = 90.00 |  = 101.17 |  = 90.00 | (degrees) |
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| Refinement: | The structure was refined using the CNS program.
The R value is
23.0
for reflections
in the resolution range 40. to
3.5 Ångstroms
. |
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