1P4K

CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	CCD
Spacegroup name	P 1
Unit cell lengths	46.176, 52.717, 61.924
Unit cell angles	80.85, 90.21, 105.08

Refinement procedure

Resolution	20.000 - 1.900
Rwork	0.182
R-free	0.21980 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.400
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.020 *	0.040 *
Total number of observations	80492 *
Number of reflections	43700 *
Completeness [%]	95.1 *	95.2 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	sparse matrix sampling method *	7.5	283 *	Cui, T., (1999) Acta Crystallogr., D55, 1961. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	Tris	10 (mM)	pH7.4
2	1	1		50 (mM)
3	1	1	EDTA	1 (mM)
4	1	1	glycine	20 (mM)
5	1	1	protein	5 (mg/ml)
6	1	2	PEG8000	8 (%)
7	1	2	PEG4000	30 (%)
8	1	2	lithium sulfate	0.2 (M)	pH8.5
9	1	2	Tris	0.1 (M)