1MEN

complex structure of human GAR Tfase and substrate beta-GAR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-08-04
Detector	MARRESEARCH
Wavelength(s)	1.1
Spacegroup name	H 3 2
Unit cell lengths	147.825, 147.825, 188.036
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	43.000 * - 2.230
Rwork	0.220
R-free	0.26700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1mej
RMSD bond length	0.008
RMSD bond angle	1.450 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.000 *	2.300
High resolution limit [Å]	2.230	2.230
Rmerge	0.076	0.510
Total number of observations	144600 *
Number of reflections	38266 *
<I/σ(I)>	24.3	2.54
Completeness [%]	98.5 *	86.4
Redundancy	3.78 *	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	4 *	PEG4000, PEG400, NaCl, Tris pH 8.5, 2mM beta-GAR, VAPOR DIFFUSION, SITTING DROP, temperature 282K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG4000	18-21 (%)
3	1	reservoir	PEG400	2 (%)
4	1	reservoir		0.1 (M)
5	1	reservoir	Tris	0.1 (M)	pH8.5