3SS5

Crystal structure of mouse Glutaminase C, L-glutamate-bound form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LNLS BEAMLINE W01B-MX2
Synchrotron site	LNLS
Beamline	W01B-MX2
Temperature [K]	100
Detector technology	CCD
Collection date	2010-09-25
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.458
Spacegroup name	P 1 21 1
Unit cell lengths	50.380, 139.430, 178.390
Unit cell angles	90.00, 93.77, 90.00

Refinement procedure

Resolution	19.985 - 2.800
R-factor	0.2082
Rwork	0.206
R-free	0.23970
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3czd
RMSD bond length	0.003
RMSD bond angle	0.708
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.7.1_743))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.880	2.950
High resolution limit [Å]	2.800	2.800
Rmerge	0.106
Number of reflections	59822
<I/σ(I)>	6	1.7
Completeness [%]	99.0	98.7
Redundancy	2.3	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	291	17% PEG3350, 0.2M NaCl, 0.1M Bis-TRIS, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K