1P4V

CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT WITH GLYCINE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Wavelength(s)	1.1001
Spacegroup name	P 1
Unit cell lengths	45.877, 52.369, 61.741
Unit cell angles	80.92, 90.41, 105.10

Refinement procedure

Resolution	20.000 - 1.900
Rwork	0.193
R-free	0.22540 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
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	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.030 *	0.080 *
Total number of observations	81010 *
Number of reflections	41067 *
Completeness [%]	95.3 *	95.3 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	sparse matrix sampling method *	7.4 *	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)