1I1L

CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200H
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1997-01-15
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	C 2 2 21
Unit cell lengths	156.090, 100.770, 141.560
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 2.400
R-factor	0.182 *
Rwork	0.182
R-free	0.22400
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.300
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000
High resolution limit [Å]	2.400	2.400 *
Rmerge	0.057 *	0.181 *
Total number of observations	132437 *
Number of reflections	42170 *
Completeness [%]	98.6 *	98.4 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	20 *	PEG400, 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	35 (mg/ml)
2	1	drop	HEPES	0.1 (M)
3	1	drop	PLP	0.010 (mM)
4	1	drop	sodium azide	1 (mM)
5	1	reservoir	PEG400	28 (%(w/v))
6	1	reservoir		0.1 (M)