1E5X

Structure of threonine synthase from Arabidopsis thaliana

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	1999-10-15
Detector	MARRESEARCH
Spacegroup name	P 1
Unit cell lengths	57.760, 62.140, 76.590
Unit cell angles	109.48, 97.61, 112.74

Refinement procedure

Resolution	29.810 - 2.250
R-factor	0.222
Rwork	0.222
R-free	0.24300
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	21.900 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SHARP
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.320
High resolution limit [Å]	2.250 *	2.200
Rmerge	0.033 *	0.183 *
Total number of observations	124846 *
Number of reflections	43719 *	6265 *
<I/σ(I)>	8.9	3
Completeness [%]	97.2	95.3
Redundancy	2.9 *	2.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5	20 *	13 % PEG 6000, 1M LICL, MES PH 6.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir		1 (M)
2	1	reservoir	PEG6000	13 (%)
3	1	reservoir	dithiothreitol	5 (mM)
4	1	reservoir	MES-KOH
5	1	drop	protein	5 (mg/ml)