1L9M

Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-08-15
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 1
Unit cell lengths	57.709, 67.515, 116.208
Unit cell angles	97.24, 90.15, 98.67

Refinement procedure

Resolution	20.000 - 2.200 *
R-factor	0.182 *
Rwork	0.182
R-free	0.22500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ggt
RMSD bond length	0.006
RMSD bond angle	25.540 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	20.000
High resolution limit [Å]	2.200 *	2.200 *
Total number of observations	521626 *
Number of reflections	75013
<I/σ(I)>	11.3
Completeness [%]	94.6 *	93

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	15 *	4%(W/V) Peg 20K, 100 mM Tris_HCl(pH 8.5), VAPOR DIFFUSION, HANGING DROP, temperature 288K
1	VAPOR DIFFUSION, HANGING DROP	8 *	15 *	4%(W/V) Peg 20K, 100 mM Tris_HCl(pH 8.5), VAPOR DIFFUSION, HANGING DROP, temperature 288K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	beta-octylglucoside	0.1 (mM)
2	1	drop	Tris-HCl	20 (mM)	pH8.0
3	1	drop	EDTA	1 (mM)
4	1	drop		125 (mM)
5	1	drop	protein	17 (mg/ml)
6	1	reservoir	PEG20000	4 (%(w/v))
7	1	reservoir	Tris-HCl	100 (mM)	pH8.5