1KNP

E. coli L-aspartate oxidase: mutant R386L in complex with succinate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-05-20
Detector	MARRESEARCH
Wavelength(s)	0.93
Spacegroup name	P 41 21 2
Unit cell lengths	72.540, 72.540, 309.120
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 2.600
R-factor	0.232 *
Rwork	0.230
R-free	0.28100 *
RMSD bond length	0.025
RMSD bond angle	2.500 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.667
High resolution limit [Å]	2.600	2.600
Rmerge	0.116	0.377
Total number of observations	100758 *
Number of reflections	22099
<I/σ(I)>	8.2	2.2
Completeness [%]	94.3	91.9 *
Redundancy	4.5	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	22 *	ispropanol, Hepes, sodium citrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	HEPES-KOH	100 (mM)	pH7.5
2	1	reservoir	sodium citrate	100 (mM)	pH7.5
3	1	reservoir	2-propanol	4-8 (%(v/v))
4	1	drop	protein	50 (mg/ml)
5	1	drop	HEPES-KOH	50 (mM)	pH8.0