2ACE

NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA

「1ACE」から置き換えられました

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	273
Detector technology	IMAGE PLATE
Collection date	1993-10
Detector	MARRESEARCH
Spacegroup name	P 31 2 1
格子定数 [Å]	112.410, 112.410, 136.700
格子定数 [度]	90.00, 90.00, 120.00

精密化法

残基	8.000 - 2.500
R因子	0.199
Rwork	0.199
R-free	0.25800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ACE
結合長の平均二乗偏差(RMSD) [Å]	0.014 *
結合角の平均二乗偏差(RMSD) [度]	1.980 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Quality characteristics

	Overall	Outer shell
分解能 [Å] (低)	25.000	2.330
分解能 [Å] (高)	2.250	2.250
Rmerge_l_obs	0.095 *	0.621 *
Total number of observations	138332 *
独立反射数	46243
<I/σ(I)>	7.4	0.9
完全性 [%]	96.6	96.7
冗長性	1.9	1.8

結晶化条件

結晶ID	方法	pH	温度	溶液条件
1	Vapor diffusion, hanging drop *	5.8	4 *	PROTEIN WAS CRYSTALLIZED FROM 35% PEG 200, 100 MM MES, PH 5.8, AT 4 DEG., temperature 277K

文献の結晶化試薬

ID	結晶ID	溶液	試薬名	濃度 (単位) (単位)	詳細
1	1	reservoir	PEG200	38 (%)
2	1	reservoir	MES	0.1 (M)
3	1	drop	protein	12 (mg/ml)