1IYD

CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL41XU
Synchrotron site	SPring-8
Beamline	BL41XU
Temperature [K]	100
Detector technology	CCD
Collection date	2000-11-26
Detector	MARRESEARCH
Wavelength(s)	1.0
Spacegroup name	C 2 2 21
Unit cell lengths	154.270, 99.020, 138.630
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.960 * - 2.150
Rwork	0.205
R-free	0.24200
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.350
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.960	2.220
High resolution limit [Å]	2.150	2.150
Rmerge	0.070 *	0.195 *
Total number of observations	324820 *
Number of reflections	58165
Completeness [%]	99.5	96.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.5	293	PEG400, HEPES, MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	40 (mg/ml)
2	1	drop	PEG400	42 (%(v/v))
3	1	drop		200 (mM)
4	1	drop	glutamate	50 (mM)
5	1	drop	sodium HEPES	100 (mM)	pH7.5
6	1	reservoir	PEG400	50 (%(v/v))
7	1	reservoir	glutarate	100 (mM)
8	1	reservoir	glutamate	50 (mM)