1IBW

STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT 25 C

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	2000-06-21
Detector	RIGAKU RAXIS IV
Spacegroup name	C 2 2 21
Unit cell lengths	97.017, 117.768, 205.789
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 3.200
R-factor	0.21086
Rwork	0.204
R-free	0.26900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pya
RMSD bond length	0.015
RMSD bond angle	2.420
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]	20.000	3.310
High resolution limit [Å]	3.200	3.200
Rmerge	0.103	0.454
Number of reflections	15945
<I/σ(I)>	10.7
Completeness [%]	80.7	84.8
Redundancy	1.8	1.8

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