1BHW
LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF XYLOSE ISOMERASE FROM MASC DATA
Summary for 1BHW
| Entry DOI | 10.2210/pdb1bhw/pdb |
| Descriptor | XYLOSE ISOMERASE (1 entity in total) |
| Functional Keywords | isomerase, masc, multiwavelength anomalous solvent contrast |
| Biological source | Actinoplanes missouriensis |
| Cellular location | Cytoplasm: P12851 |
| Total number of polymer chains | 4 |
| Total formula weight | 173589.86 |
| Authors | Ramin, M.,Shepard, W.,Fourme, R.,Kahn, R. (deposition date: 1998-06-10, release date: 1998-11-04, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 10089406DOI: 10.1107/S090744499800626X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.1 Å) |
Structure validation
Download full validation report
