000 | 02012 a2200541 4500 | ||
---|---|---|---|
005 | 20250517130124.0 | ||
264 | 0 | _c20171127 | |
008 | 201711s 0 0 eng d | ||
022 | _a2053-230X | ||
024 | 7 |
_a10.1107/S2053230X16018525 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aCala, Ali R | |
245 | 0 | 0 |
_aThe crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 Å resolution. _h[electronic resource] |
260 |
_bActa crystallographica. Section F, Structural biology communications _c12 2016 |
||
300 |
_a885-891 p. _bdigital |
||
500 | _aPublication Type: Journal Article | ||
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 |
_aBacterial Proteins _xchemistry |
650 | 0 | 4 |
_aBartonella henselae _xchemistry |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 | _aCloning, Molecular |
650 | 0 | 4 | _aCrystallography, X-Ray |
650 | 0 | 4 |
_aDihydrodipicolinate Reductase _xchemistry |
650 | 0 | 4 |
_aEscherichia coli _xgenetics |
650 | 0 | 4 | _aGene Expression |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 |
_aNADP _xchemistry |
650 | 0 | 4 |
_aPlasmids _xchemistry |
650 | 0 | 4 | _aProtein Binding |
650 | 0 | 4 | _aProtein Conformation, alpha-Helical |
650 | 0 | 4 | _aProtein Conformation, beta-Strand |
650 | 0 | 4 | _aProtein Interaction Domains and Motifs |
650 | 0 | 4 | _aProtein Multimerization |
650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
650 | 0 | 4 | _aSequence Alignment |
650 | 0 | 4 | _aSequence Homology, Amino Acid |
650 | 0 | 4 | _aSubstrate Specificity |
700 | 1 | _aNadeau, Maria T | |
700 | 1 | _aAbendroth, Jan | |
700 | 1 | _aStaker, Bart L | |
700 | 1 | _aReers, Alexandra R | |
700 | 1 | _aWeatherhead, Anthony W | |
700 | 1 | _aDobson, Renwick C J | |
700 | 1 | _aMyler, Peter J | |
700 | 1 | _aHudson, André O | |
773 | 0 |
_tActa crystallographica. Section F, Structural biology communications _gvol. 72 _gno. Pt 12 _gp. 885-891 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1107/S2053230X16018525 _zAvailable from publisher's website |
999 |
_c26666678 _d26666678 |