1BHW

LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF XYLOSE ISOMERASE FROM MASC DATA

1BHW の概要

• エントリーDOI: 10.2210/pdb1bhw/pdb
• 分子名称: XYLOSE ISOMERASE (1 entity in total)
• 機能のキーワード: isomerase, masc, multiwavelength anomalous solvent contrast
• 由来する生物種: Actinoplanes missouriensis
• 細胞内の位置: Cytoplasm: P12851
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 173589.86

構造登録者

Ramin, M.,Shepard, W.,Fourme, R.,Kahn, R. (登録日: 1998-06-10, 公開日: 1998-11-04, 最終更新日: 2024-05-22)

主引用文献

Ramin, M.,Shepard, W.,Fourme, R.,Kahn, R.
Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values.
Acta Crystallogr.,Sect.D, 55:157-167, 1999

PubMed Abstract: A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48] presented the theoretical foundations of MASC, a new contrast-variation method using multiwavelength anomalous scattering, and reported the first experimental results. New experiments have been conducted both at the ESRF (Grenoble, France) and at LURE-DCI (Orsay, France), using cryocooled crystals of three proteins of known structures and very different molecular weights. Amplitudes of {GammaT(h)}, the 'normal' structure factors of the anomalously scattering part of the crystal including the solvent zone and the ordered anomalous scattering sites (if any), have been extracted from multiwavelength data. In the very low resolution range (d >/= 20 A), the agreement between experimental {GammaT(h)} and model values calculated from the bulk solvent is all the more satisfactory since the molecular weight of the protein is high. For spacings between 10 and 20 A, the agreement between experimental {GammaT(h)} and model values is also satisfactory if one takes into account ordered anomalous scatterer sites. Such sites have been found in the three cases.

PubMed: 10089406
DOI: 10.1107/S090744499800626X

実験手法

X-RAY DIFFRACTION (4.1 Å)