1R43

Crystal structure of beta-alanine synthase from Saccharomyces kluyveri (selenomethionine substituted protein)

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2002-10-03
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9793, 0.9794, 0.9393
Spacegroup name	P 1 21 1
Unit cell lengths	60.430, 77.630, 110.570
Unit cell angles	90.00, 95.63, 90.00

Refinement procedure

Resolution	30.000 * - 2.800
R-factor	0.21388
Rwork	0.211
R-free	0.28100 *
Structure solution method	MAD
RMSD bond length	0.009 *
RMSD bond angle	1.200 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SOLVE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.950
High resolution limit [Å]	2.800	2.800
Rmerge	0.119 *	0.490 *
Number of reflections	25306
<I/σ(I)>	15.5	3.2
Completeness [%]	99.9	100
Redundancy	3.8 *	3.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	20 *	trisodium citrate, dioxane, DTT, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	4.0-4.5 (mg/ml)
2	1	drop	Tris	50 (mM)	pH7.5
3	1	drop	dithiothreitol	1 (mM)
4	1	drop		100 (mM)
5	1	reservoir	trisodium citrate	1.0 (M)
6	1	reservoir	MES	0.1 (M)	pH6.5
7	1	reservoir	dioxane	5 (%(v/v))