1K75

The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X8C
Synchrotron site	NSLS
Beamline	X8C
Temperature [K]	100
Detector technology	CCD
Collection date	2000-07-15
Detector	ADSC QUANTUM 4
Wavelength(s)	0.97950,0.97934,0.97857
Spacegroup name	P 21 21 21
Unit cell lengths	54.370, 107.520, 157.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 1.750
R-factor	0.19 *
Rwork	0.190
R-free	0.22500
Structure solution method	MAD
RMSD bond length	0.013
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	1.780
High resolution limit [Å]	1.750	1.750
Rmerge	0.060 *	0.276 *
Total number of observations	402344 *
Number of reflections	91330 *
<I/σ(I)>	11.4	2.2
Completeness [%]	97.3	79.7
Redundancy	4.4	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	18 *	PEG 3350, glycerol, imidazole/malic acid buffer, ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15.4 (mg/ml)
2	1	drop	Tris-Cl	20 (mM)	pH7.5
3	1	drop		0.2 (M)
4	1	drop	dithiothreitol	5 (mM)
5	1	drop	L-histidine	1 (mM)
6	1	reservoir	PEG3350	20 (%(w/v))
7	1	reservoir	glycerol	7 (%(v/v))
8	1	reservoir	imidazole-malic acid	0.1 (M)	pH5.5
9	1	reservoir	ammonium sulfate	0.2 (M)