Crystallization and preliminary X-ray crystallographic analysis of acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa.
Acetohydroxy acid isomeroreductase (AHIR) is involved in the biosynthetic pathway of branched-chain amino acids in microorganisms and plants. AHIR from Pseudomonas aeruginosa has been overexpressed in Escherichia coli and crystallized at 297 K using potassium/sodium tartrate as a precipitant. X-ray diffraction data have been collected to 2.0 A resolution at 100 K using synchrotron radiation. The crystals belong to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 184.38 A, alpha = beta = gamma = 90 degrees. Six monomers are present in the asymmetric unit, giving a V(M) of 2.34 A(3) Da(-1) and a solvent content of 47.4%.
Eom
Su Jeong
SJ
Structural Proteomics Laboratory, School of Chemistry and Molecular Engineering, Seoul National University, Seoul 151-742, South Korea.
Ahn
Hyung Jun
HJ
Yoon
Hye Jin
HJ
Lee
Byung Il
BI
Bae
Seung Hee
SH
Baek
Seung Hun
SH
Suh
Se Won
SW
D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D050540:Ketol-Acid Reductoisomerase; D008027:Light; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry; D012542:Scattering, Radiation
D011994:Recombinant Proteins; D000429:Alcohol Oxidoreductases; D050540:Ketol-Acid Reductoisomerase