1WOO

Crystal structure of T-protein of the Glycine Cleavage System

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	PAL/PLS BEAMLINE 6B
Synchrotron site	PAL/PLS
Beamline	6B
Temperature [K]	100
Detector technology	CCD
Collection date	2004-06-08
Detector	BRUKER
Wavelength(s)	1.12714
Spacegroup name	P 21 21 21
Unit cell lengths	52.499, 53.942, 149.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.510 - 2.400
R-factor	0.218
Rwork	0.218
R-free	0.27500
Structure solution method	Crystal 1 SINGLE WAVELENGTH PROTOCOL, Crysatl 2 MAD PROTOCOL
RMSD bond length	0.008
RMSD bond angle	1.300
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SHELXS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.490
High resolution limit [Å]	2.400	2.400
Number of reflections	17533
Completeness [%]	98.3	91.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.25	297	PEG 3350, sodium dihydrogen phosphate, pH 4.25, VAPOR DIFFUSION, HANGING DROP, temperature 297K
1	VAPOR DIFFUSION, HANGING DROP	4.25	297	PEG 3350, sodium dihydrogen phosphate, pH 4.25, VAPOR DIFFUSION, HANGING DROP, temperature 297K