1PVN

The crystal structure of the complex between IMP dehydrogenase catalytic domain and a transition state analogue MZP

Replaces:  1MWF

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-C
Synchrotron site	APS
Beamline	14-BM-C
Temperature [K]	100
Detector technology	CCD
Collection date	2001-09-23
Detector	ADSC QUANTUM 4
Wavelength(s)	1.000
Spacegroup name	P 21 21 21
Unit cell lengths	96.754, 112.566, 159.756
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 * - 2.000
R-factor	0.196
Rwork	0.196
R-free	0.22200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Tetramer of IMP dehydrogenase PDB entry 1LRT
RMSD bond length	0.006 *
RMSD bond angle	1.280 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.069	0.181
Total number of observations	1775920 *
Number of reflections	113342 *
<I/σ(I)>	22	7.8
Completeness [%]	99.1	99.9
Redundancy	16

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	298	PEG 10,000, MES, Glycerol, KCl, Tris, pH 6.25, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.0 (mg/ml)
10	1	reservoir	dithiothreitol	1 (mM)
2	1	drop	Tris-HCl	20 (mM)	pH7.5
3	1	drop	glycerol	5 (%)
4	1	drop	MZP	0.6 (mM)
5	1	drop	dithiothreitol	1 (mM)
6	1	reservoir	PEG10000	10 (%)
7	1	reservoir	MES	100 (mM)	pH6.25
8	1	reservoir		120 (mM)
9	1	reservoir	glycerol	20 (%)