3NRR

Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2010-05-21
Detector	ADSC QUANTUM 315
Wavelength(s)	0.99740
Spacegroup name	P 1
Unit cell lengths	51.330, 83.830, 83.920
Unit cell angles	119.61, 102.04, 90.26

Refinement procedure

Resolution	19.940 - 1.800
R-factor	0.1956
Rwork	0.194
R-free	0.23600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3k2h
RMSD bond length	0.016
RMSD bond angle	1.753
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASES
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.830
High resolution limit [Å]	1.800	4.880	1.800
Rmerge	0.060	0.033	0.354
Number of reflections	108796
<I/σ(I)>	12.3		2.439
Completeness [%]	97.2	99.4	95.9
Redundancy	2	2	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	1:1 CO-CRYSTALLIZATION DROP. PROTEIN SOLUTION: 20 MG/ML PROTEIN, 2.0MM DUMP, 2.0MM NADP, 5.0MM RALTITREXED, 0.5M SODIUM CHLORIDE, 0.025M HEPES, 5%(V/V) GLYCEROL, 2.0MM DITHIOTHREITOL. CRYSTALLANT SOLUTION (HT INDEX E11): 0.02M MAGNESIUM CHLORIDE HEXAHYDRATE, 0.1M HEPES, 22%(W/V) POLY(ACRYLIC ACID) SODIUM SALT 5100, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K