1IU9

Crystal structure of the C-terminal domain of aspartate racemase from Pyrococcus horikoshii OT3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Temperature [K]	90
Detector technology	CCD
Collection date	2001-02-28
Detector	MARRESEARCH
Wavelength(s)	1.000
Spacegroup name	P 21 21 21
Unit cell lengths	36.829, 45.328, 57.366
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	100.000 * - 2.040
R-factor	0.225
Rwork	0.225
R-free	0.27100 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	C-terminal domain in the intact structure of aspartate racemase from Pyrococcus horikoshii OT3
RMSD bond length	0.005
RMSD bond angle	1.070 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000 *	2.150
High resolution limit [Å]	2.040	2.040
Rmerge	0.108	0.252
Total number of observations	57302 *
Number of reflections	6508 *
<I/σ(I)>	5.2	3
Completeness [%]	99.3	96.3
Redundancy	5.4	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8 *	20 *	16% Peg8000, 0.10M MES, 0.2M Calcium acetate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.2K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	30 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)	pH8.0
3	1	drop	mercaptoethanol	2 (mM)
4	1	reservoir	PEG8000	16 (%)
5	1	reservoir	MES	0.10 (M)	pH6.5
6	1	reservoir	calcium acetate	0.20 (M)