1IBT

STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT-170 C

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	103
Detector technology	IMAGE PLATE
Collection date	1999-03-01
Detector	RIGAKU RAXIS IV
Spacegroup name	C 2 2 21
Unit cell lengths	96.200, 115.309, 202.386
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.600
R-factor	0.266
Rwork	0.260
R-free	0.31700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pya
RMSD bond length	0.017
RMSD bond angle	3.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	2.670
High resolution limit [Å]	2.600 *	2.580
Rmerge	0.089	0.389
Number of reflections	34308
<I/σ(I)>	14.1
Completeness [%]	97.0	90.5
Redundancy	2.7	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	298	PEG 400, PEG 4000, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	reservoir	PEG400	0-15 (%)
3	1	reservoir	PEG4000	4-8 (%)
4	1	reservoir	sodium acetate	0.1 (M)	pH4.6