温度: 298 K / 手法: 蒸気拡散法, ハンギングドロップ法 / pH: 7 詳細: Prior to crystallization the enzyme was dialyzed into 40 mM KH2PO4, 2.0 mM 2-mercaptoethanol, 0.2 mM EDTA, pH 7.0 for 24 hours. Single crystals of the K244N mutant were obtained by mixing a ...詳細: Prior to crystallization the enzyme was dialyzed into 40 mM KH2PO4, 2.0 mM 2-mercaptoethanol, 0.2 mM EDTA, pH 7.0 for 24 hours. Single crystals of the K244N mutant were obtained by mixing a 20 mg/ml filtered solution (0.22 m) of the K244N enzyme with a solution of 17% (w/v) PEG 1450, 50 mM malonate, 0.2 mM EDTA, 1 mM sodium azide and 20 mM Bis-Tris buffer pH 7.0 in a 1:1 ratio (v/v), VAPOR DIFFUSION, HANGING DROP, temperature 298K
解像度: 2.59→2.68 Å / 冗長度: 2.62 % / Rmerge(I) obs: 0.327 / Mean I/σ(I) obs: 12.2 / % possible all: 89.8
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解析
ソフトウェア
名称
バージョン
分類
REFMAC
5.1.24
精密化
DENZO
データ削減
SCALEPACK
データスケーリング
AMoRE
位相決定
精密化
構造決定の手法: 分子置換 開始モデル: A consensus model using overlayed previously published pdb entry 1EZZ (mutant P268A catalytic chain) and 1NBE (T82A regulatory chain) and wild type 3AT1 was used.
解像度: 2.6→29.55 Å / Cor.coef. Fo:Fc: 0.888 / Cor.coef. Fo:Fc free: 0.81 / SU B: 10.082 / SU ML: 0.227 / TLS residual ADP flag: LIKELY RESIDUAL Isotropic thermal model: Isotropic thermal model was retained for individual atoms in final runs but global anisotropic assignment for domains (TLS) 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 1.267 / ESU R Free: 0.335 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD / 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
反射数
%反射
Selection details
Rfree
0.23117
1589
4.9 %
RANDOM
Rwork
0.20122
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obs
0.20186
30529
89.44 %
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all
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36343
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溶媒の処理
イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.4 Å / 溶媒モデル: BABINET MODEL WITH MASK