It is demonstrated that standard in-house protein crystal X-ray diffraction apparatus can be used to measure very low resolution reflections with only a few modifications. The apparatus and modifications are described in detail and tested on two different macromolecular crystal samples: lysozyme and the 30S ribosomal subunit. Contrast-variation measurements on tetragonal hen egg-white lysozyme demonstrate the potential usefulness of the apparatus in providing accurate data for the determination of macromolecular envelopes. In contrast, the measurement of very low resolution diffraction from crystals of the 30S ribosome subunit illustrates how in-house facilities can provide data from small weakly diffracting crystals of a very large macromo...
We describe the technical aspects of the in-situ X-ray diffraction of a protein crystal prepared by ...
AbstractThe x-ray exposure at which significant radiation damage occurs has been quantified for froz...
The components of monochromatic diffractometer suitable for data collection on crystals of biologica...
X-ray diffraction plays a pivotal role in the understanding of biological systems by revealing atomi...
An analysis is given of the effect of different beam and detector parameters on the sharpness of rec...
The generation of high quality diffracting crystals remains an area that requires considerable perso...
A crystal of hen egg white lysozyme was analyzed by means of energy dispersive X ray Laue diffracti...
145 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2005.The determination of the atom...
X-ray diffraction data have been collected at both low (120 K) and room temperature from triclinic c...
Proteins are remarkable molecular machines that are essential for life. They can do many things rang...
Recent developments in serial crystallography at X-ray free electron lasers (XFELs) and synchrotrons...
The technique of X-ray diffraction is central to our understanding of biomolecular structure at high...
The three-dimensional structures of macromolecules and their complexes are mainly elucidated by X-ra...
To date X-ray protein crystallography is the most successful technique available for the determinati...
We describe the technical aspects of the in-situ X-ray diffraction of a protein crystal prepared by ...
AbstractThe x-ray exposure at which significant radiation damage occurs has been quantified for froz...
The components of monochromatic diffractometer suitable for data collection on crystals of biologica...
X-ray diffraction plays a pivotal role in the understanding of biological systems by revealing atomi...
An analysis is given of the effect of different beam and detector parameters on the sharpness of rec...
The generation of high quality diffracting crystals remains an area that requires considerable perso...
A crystal of hen egg white lysozyme was analyzed by means of energy dispersive X ray Laue diffracti...
145 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2005.The determination of the atom...
X-ray diffraction data have been collected at both low (120 K) and room temperature from triclinic c...
Proteins are remarkable molecular machines that are essential for life. They can do many things rang...
Recent developments in serial crystallography at X-ray free electron lasers (XFELs) and synchrotrons...
The technique of X-ray diffraction is central to our understanding of biomolecular structure at high...
The three-dimensional structures of macromolecules and their complexes are mainly elucidated by X-ra...
To date X-ray protein crystallography is the most successful technique available for the determinati...
We describe the technical aspects of the in-situ X-ray diffraction of a protein crystal prepared by ...
AbstractThe x-ray exposure at which significant radiation damage occurs has been quantified for froz...
The components of monochromatic diffractometer suitable for data collection on crystals of biologica...