1HG1

X-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and D-aspartate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X9B
Synchrotron site	NSLS
Beamline	X9B
Temperature [K]	100
Detector technology	CCD
Collection date	2000-11-15
Detector	ADSC CCD
Spacegroup name	C 1 2 1
Unit cell lengths	105.840, 90.425, 126.893
Unit cell angles	90.00, 91.80, 90.00

Refinement procedure

Resolution	20.000 - 1.800
R-factor	0.179
Rwork	0.179
R-free	0.20400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PREVIUOSLY PUBLISHED STRUCTURE OF ERWINIA CHRYSANTHEMI L-ASPARAGINSE (MILLER ET AL. FEBS LETT. 1993
RMSD bond length	0.005
RMSD bond angle	23.020 *
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.082 *	0.530 *
Total number of observations	331851 *
Number of reflections	100021
<I/σ(I)>	7.4	2.1
Completeness [%]	90.1	74.7
Redundancy	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.4		Miller, M., (1993) FEBS Lett., 328, 275. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	50 (%)
2	1	reservoir	CHES	0.1 (M)
3	1	reservoir	PEG400	2 (%(w/v))