2GB3

Crystal structure of Aspartate aminotransferase (tm1698) from Thermotoga maritima at 2.50 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	100
Detector technology	CCD
Collection date	2005-04-28
Detector	ADSC QUANTUM 315
Spacegroup name	P 1 21 1
Unit cell lengths	75.094, 214.051, 76.839
Unit cell angles	90.00, 112.31, 90.00

Refinement procedure

Resolution	107.030 - 2.500
R-factor	0.231
Rwork	0.229
R-free	0.26600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1xi9A
RMSD bond length	0.010
RMSD bond angle	1.526
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	107.211	107.210	2.560
High resolution limit [Å]	2.496	11.160	2.500
Rmerge	0.139	0.057	0.200
Total number of observations		3894	9584
Number of reflections	75747	888	5158
<I/σ(I)>	3.4	5.3	3.5
Completeness [%]	97.5	98.8	89.4
Redundancy	3.4	4.4	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP, NANODROP	4.5	277	35.0% 2-propanol, 0.1M Acetate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K