3PPL

Crystal structure of an aspartate transaminase (NCgl0237, Cgl0240) from CORYNEBACTERIUM GLUTAMICUM ATCC 13032 KITASATO at 1.25 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	100
Detector technology	CCD
Collection date	2010-02-11
Detector	MARMOSAIC 325 mm CCD
Wavelength(s)	0.91837,0.97944,0.97908
Spacegroup name	C 1 2 1
Unit cell lengths	97.755, 54.424, 176.340
Unit cell angles	90.00, 101.60, 90.00

Refinement procedure

Resolution	29.324 - 1.250
R-factor	0.1059
Rwork	0.105
R-free	0.12420
Structure solution method	MAD
RMSD bond length	0.014
RMSD bond angle	1.598
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHELX
Refinement software	REFMAC (5.5.0110)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.324		1.290
High resolution limit [Å]	1.250	2.690	1.250
Rmerge	0.035	0.020	0.276
Number of reflections	241991	45633	37606
<I/σ(I)>	13.04	32.1	2.75
Completeness [%]	92.1	92.2	84.8
Redundancy	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.2	293	0.2M sodium chloride, 20.0% polyethylene glycol 8000, 0.1M phosphate-citrate pH 4.2, Additive: 0.001 M alpha-ketoglutaric acid, NANODROP', VAPOR DIFFUSION, SITTING DROP, temperature 293K