4ND4

Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (pyruvic acid) and cofactor (b-nicotinamide adenine dinucleotide)

Replaces:  2FM3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2004-07-02
Detector	MARRESEARCH
Wavelength(s)	0.9998
Spacegroup name	P 32 2 1
Unit cell lengths	95.905, 95.905, 185.723
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.640 - 2.200
R-factor	0.20275
Rwork	0.201
R-free	0.22277
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2EWD
RMSD bond length	0.004
RMSD bond angle	0.961
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.081	0.303
Number of reflections	50964
Completeness [%]	100.0	99.9
Redundancy	7.4	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	277	The protein was incubated with 1 mM pyruvate and 100 uM APAD+ for 1 hour on ice prior to crystallization. Reservoir solution was 1.45-1.65 M ammonium sulfate in 0.1 M sodium cacodylate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K