7EYC

Crystal structure of Tau and acetylated tau peptide antigen

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PAL/PLS BEAMLINE 7A (6B, 6C1)
Synchrotron site	PAL/PLS
Beamline	7A (6B, 6C1)
Temperature [K]	100
Detector technology	CCD
Collection date	2020-09-28
Detector	ADSC QUANTUM 270
Wavelength(s)	0.9730
Spacegroup name	P 21 21 21
Unit cell lengths	76.599, 83.862, 134.371
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.810 - 2.490
R-factor	0.1948
Rwork	0.192
R-free	0.24520
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4lex
RMSD bond length	0.011
RMSD bond angle	1.505
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.8.0238)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.540
High resolution limit [Å]	2.489	6.780	2.500
Rmerge	0.075	0.047	0.422
Rmeas	0.083	0.052	0.464
Rpim	0.035	0.023	0.191
Number of reflections	30917	1682	1521
<I/σ(I)>	13
Completeness [%]	99.9	99.1	99.9
Redundancy	5.5	4.8	5.6
CC(1/2)		0.997	0.916

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		291	70% (+/-)-2-Methyl-2,4-pentanediol, 0.1 M HEPES, pH 7.5, 10 mM Calcium chloride