| 000 | 01725 a2200505 4500 | ||
|---|---|---|---|
| 005 | 20250513205027.0 | ||
| 264 | 0 | _c20000411 | |
| 008 | 200004s 0 0 eng d | ||
| 022 | _a0036-8075 | ||
| 024 | 7 |
_a10.1126/science.287.5462.2482 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aKeck, J L | |
| 245 | 0 | 0 |
_aStructure of the RNA polymerase domain of E. coli primase. _h[electronic resource] |
| 260 |
_bScience (New York, N.Y.) _cMar 2000 |
||
| 300 |
_a2482-6 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAmino Acid Motifs |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aCatalytic Domain |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 |
_aDNA Helicases _xchemistry |
| 650 | 0 | 4 |
_aDNA Primase _xchemistry |
| 650 | 0 | 4 | _aDNA Replication |
| 650 | 0 | 4 |
_aDNA, Bacterial _xmetabolism |
| 650 | 0 | 4 |
_aDNA, Single-Stranded _xmetabolism |
| 650 | 0 | 4 |
_aDNA-Directed RNA Polymerases _xchemistry |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 |
_aMetals _xmetabolism |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aNucleic Acid Hybridization |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 |
_aRNA _xbiosynthesis |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 | _aTemplates, Genetic |
| 700 | 1 | _aRoche, D D | |
| 700 | 1 | _aLynch, A S | |
| 700 | 1 | _aBerger, J M | |
| 773 | 0 |
_tScience (New York, N.Y.) _gvol. 287 _gno. 5462 _gp. 2482-6 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1126/science.287.5462.2482 _zAvailable from publisher's website |
| 999 |
_c10695400 _d10695400 |
||