Details

Autor(en) / Beteiligte

• Vellieux, F. M. D.
• Kalk, K. H.
• Drenth, J.
• Hol, W. G. J.

Titel

Structure determination of quinoprotein methylamine dehydrogenase from Thiobacillus versutus

Ist Teil von

• Acta crystallographica. Section B, Structural science, 1990-12, Vol.46 (6), p.806-823

Ort / Verlag

5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography

Erscheinungsjahr

1990

Quelle

MEDLINE

Beschreibungen/Notizen

• The crystal structure of quinoprotein methylamine dehydrogenase from Thiobacillus versutus (EC 1.4.99.3, Mr = 123,500) has been solved to 2.25 A resolution. The crystals of space group P3(1)21 (a = b = 129.8, c = 104.3 A) contain half a tetrameric enzyme molecule in the asymmetric unit, with a solvent content of ca 70%. The procedure used to solve this structure involved multiple isomorphous-replacement phasing, complemented by phase extension using solvent flattening, and phase combination with partial-model phases. The use of solvent flattening was essential to generate good quality electron density maps into which initial models were built. These partial models were refined using molecular-dynamics procedures. Refined model phases were then combined with solvent-flattening phases to generate improved electron density distributions. In the absence of an amino-acid sequence for this enzyme, the current 2.25 A resolution electron density map was interpreted to provide a model for the complete molecule. The crystallographic R factor for this model, which lacks any water molecules, is 28.6% for data between 6.0 and 2.25 A resolution.