2AAJ

Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2003-09-19
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 21 3
Unit cell lengths	110.152, 110.152, 110.152
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.400 - 2.740
R-factor	0.1641
Rwork	0.161
R-free	0.21330
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	wildtype MSAD
RMSD bond length	0.021
RMSD bond angle	1.923
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.400	2.860
High resolution limit [Å]	2.740	2.740
Rmerge	0.129	0.391
Number of reflections	11976
<I/σ(I)>	9.2
Completeness [%]	99.4	98.7
Redundancy	12.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	298	2.8 M Li(CH3COO), 0.7 M (NH4)2SO4, and 100 mM sodium citrate buffer (pH 5.5), VAPOR DIFFUSION, SITTING DROP, temperature 298K