PROBABLEWRKYTRANSCRIPTIONFACTOR52 / DISEASE RESISTANCE PROTEIN RRS1 / DISEASE RESISTANCE PROTEIN SLH1 / PROTEIN SENSITIVE TO LOW ...DISEASE RESISTANCE PROTEIN RRS1 / DISEASE RESISTANCE PROTEIN SLH1 / PROTEIN SENSITIVE TO LOW HUMIDITY 1 / RESISTANCE TO RALSTONI A SOLANACEARUM 1 PROTEIN / WRKY DNA-BINDING PROTEIN 52
プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
波長: 0.9539 Å / 相対比: 1
反射
解像度: 2.65→29.84 Å / Num. obs: 32619 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / 冗長度: 23 % / Biso Wilson estimate: 73.73 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 27.5
反射 シェル
解像度: 2.65→2.78 Å / 冗長度: 24 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 2 / % possible all: 100
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解析
ソフトウェア
名称
バージョン
分類
PHENIX
(PHENIX.REFINE)
精密化
XDS
データ削減
Aimless
データスケーリング
PHASER
位相決定
精密化
構造決定の手法: 分子置換 開始モデル: RPS4 TIR AND RRS1 TIR 解像度: 2.65→29.794 Å / SU ML: 0.36 / σ(F): 1.34 / 位相誤差: 21.13 / 立体化学のターゲット値: ML 詳細: CRYSTALS OF THE RRS1 AND RPS4 TIR DOMAIN HETERODIMER WERE OBTAINED BY LINKING RRS1(6-153) AND RPS4(10-178) WITH A FIVE-RESIDUE (GSGGS) LINKER . A REGION ENCOMPASSING 11 RESIDUES INCLUDING THE ...詳細: CRYSTALS OF THE RRS1 AND RPS4 TIR DOMAIN HETERODIMER WERE OBTAINED BY LINKING RRS1(6-153) AND RPS4(10-178) WITH A FIVE-RESIDUE (GSGGS) LINKER . A REGION ENCOMPASSING 11 RESIDUES INCLUDING THE LINKER COULD NOT BE MODELED DUE TO THE LACK OF INTERPRETABLE ELECTRON DENSITY. WE FAVOR THE INTERPRETATION THAT THE LINKED CHAIN OCCURS BETWEEN MOLECULES A-D, B-C. HOWEVER, AS IT IS NOT POSSIBLE TO MODEL THE LINKER REGION WITH CERTAINTY WE CANNOT EXPLICITLY DETERMINE WHICH MOLECULES ARE LINKED IN THE CRYSTAL. FOR THIS REASON, WE HAVE LABELLED THE RRS1 AND RPS4 TIR DOMAIN MOLECULES AS SEPARATE CHAINS IN THE COORDINATE FILE DEPOSITED. THE FUNCTIONALLY IMPORTANT HETERODIMERISATION INTERFACE BETWEEN RRS1 AND RPS4 TIR DOMAINS OCCURS BETWEEN PROTEIN CHAINS A-B AND C-D.
Rfactor
反射数
%反射
Rfree
0.2267
1997
6.1 %
Rwork
0.1823
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obs
0.185
32498
99.98 %
溶媒の処理
減衰半径: 0.9 Å / VDWプローブ半径: 1.11 Å / 溶媒モデル: FLAT BULK SOLVENT MODEL