3ECD

Crystal structure of serine hydroxymethyltransferase from Burkholderia pseudomallei

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Collection date	2008-08-23
Wavelength(s)	0.99994
Spacegroup name	P 1
Unit cell lengths	58.212, 61.865, 117.577
Unit cell angles	97.79, 89.97, 110.24

Refinement procedure

Resolution	58.222 - 1.600
R-factor	0.188
Rwork	0.187
R-free	0.20600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1kkj
RMSD bond length	0.008
RMSD bond angle	1.200
Data reduction software	MOSFLM
Data scaling software	SCALA (3.2.25)
Phasing software	MOLREP
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	58.222	58.220	1.690
High resolution limit [Å]	1.400	5.060	1.600
Rmerge	0.044	0.021	0.408
Total number of observations		13967	54497
Number of reflections	190206
<I/σ(I)>	12.358	26.2	1.8
Completeness [%]	94.6	99	86.4
Redundancy	2.1	2.2	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	289	PACT SCREEN CONDITION C6, 20% PEG 6000, 0.2 M NaCl, 0.1 M HEPES-KOH pH 7.0, 24.1 mg/mL protein, 0.4/0.4 uL drops, Crystal ID 109933C6, VAPOR DIFFUSION, SITTING DROP, temperature 289K