1KTA

HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE : THREE DIMENSIONAL STRUCTURE OF THE ENZYME IN ITS PYRIDOXAMINE PHOSPHATE FORM.

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	69.450, 105.308, 107.829
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 1.900
Rwork	0.240
R-free	0.28700
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.018
RMSD bond angle	24.800 *
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]	20.000	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.057	0.403
Total number of observations	246448 *
Number of reflections	62273
<I/σ(I)>	0.215	0.022
Completeness [%]	98.4	91.1
Redundancy	1.6	1.6

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)