1RAI

CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY

Experimental procedure

Spacegroup name	P 3 2 1
Unit cell lengths	122.130, 122.130, 142.510
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	? - 2.500
R-factor	0.182
Rwork	0.182
RMSD bond length	0.018
RMSD bond angle	3.720
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
Low resolution limit [Å]	10.000 *
High resolution limit [Å]	2.500 *
Rmerge	0.097 *
Total number of observations	169691 *
Number of reflections	35204 *
Completeness [%]	82.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	5.8 *		taken from Gouaux, J. E. et al (1989). Biochemistry, 28, 1798-1803. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	enzyme	20 (mg/ml)
2	1	2	sodium citrate	40 (mM)
3	1	2	beta-mercaptoethanol	1.0 (mM)
4	1	2	EDTA	0.2 (mM)
5	1	2	cytidine 5'-triphosphate	1.0 (mM)