2FZG

The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.25 Resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	2005-03-25
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 3 2 1
Unit cell lengths	119.940, 119.940, 141.970
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	28.230 - 2.250
R-factor	0.201
Rwork	0.201
R-free	0.23700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1za2
Data reduction software	d*TREK
Data scaling software	d*TREK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	28.230	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.090	0.424
Number of reflections	79872
<I/σ(I)>	9.7	3.9
Completeness [%]	99.8	99.6
Redundancy	4.62	4.24

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICRODIALYSIS	5.7	298	ATCase holoenzyme was crystallized by microdialysis, using 50 L wells. The enzyme solution, at ~18 mg/mL, was dialyzed against a solution of 40 mM citric acid, 3 mM sodium azide, 1 mM 2-mercaptoethanol, 1 mM cytidine 5 -triphosphate, 0.2 mM EDTA (pH 5.7), MICRODIALYSIS, temperature 298K