1KT8

HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL): THREE DIMENSIONAL STRUCTURE OF ENZYME IN ITS KETIMINE FORM WITH THE SUBSTRATE L-ISOLEUCINE

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]	223
Detector technology	CCD
Collection date	1999-04-20
Spacegroup name	P 21 21 21
Unit cell lengths	69.475, 105.457, 107.429
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.700 * - 1.900
Rwork	0.243
R-free	0.28400
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.019
RMSD bond angle	24.600 *
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]	19.700 *	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.069	0.666 *
Total number of observations	238575 *
Number of reflections	61939 *
<I/σ(I)>	5.4
Completeness [%]	95.6	90.3 *
Redundancy	4.7	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7		Yennawar, N., (2001) Acta Crystallogr., Sect.D, 57, 506. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.5 (mg/ml)
2	1	drop	HEPES	50 (mM)
3	1	drop	dithiothreitol	20 (mM)
4	1	drop	EDTA	50 (mM)
5	1	reservoir	PEG1500	22-30 (%)
6	1	reservoir	HEPES	100 (mM)
7	1	reservoir	dithiothreitol	20 (mM)