Biological Crystallography

 

Acta Cryst. (2000). D56, 1205-1214  [ doi:10.1107/S0907444900009355 ]

Direct methods and protein crystallography at low resolution

C. J. Gilmore

Synopsis: This paper discusses how the phase problem in protein crystallography needs atomic resolution data for ab initio model-free phasing to work.

Online October 2000

 

Acta Cryst. (2000). D56, 1215-1222  [ doi:10.1107/S0907444900010787 ]

Macromolecular structure determination by cryo-electron microscopy

H. R. Saibil

Synopsis: This paper reviews the contribution and future potential of cryo-electron microscopy and three-dimensional reconstruction in the determination of macromolecular structures.

Online October 2000

 

Acta Cryst. (2000). D56, 1223-1232  [ doi:10.1107/S0907444900010088 ]

Low-resolution ab initio phasing: problems and advances

V. Y. Lunin, N. L. Lunina, T. E. Petrova, T. P. Skovoroda, A. G. Urzhumtsev and A. D. Podjarny

Synopsis: A low-resolution phasing statistical approach is presented and figures of merit which may be used successfully for phasing are discussed.

Online October 2000

 

Acta Cryst. (2000). D56, 1233-1244  [ doi:10.1107/S0907444900009331 ]

Density constraints and low-resolution phasing

A. G. Urzhumtsev, N. L. Lunina, T. P. Skovoroda, A. D. Podjarny and V. Y. Lunin

Synopsis: Applications of different density constraints in low-resolution phasing are discussed.

Online October 2000

 

Acta Cryst. (2000). D56, 1245-1252  [ doi:10.1107/S0907444900009343 ]

Ab initio low-resolution phasing in crystallography of macromolecules by maximization of likelihood

T. E. Petrova, V. Y. Lunin and A. D. Podjarny

Synopsis: The possibility of using the statistical likelihood as a figure of merit in low-resolution ab initio phasing is tested.

Online October 2000

 

Acta Cryst. (2000). D56, 1253-1258  [ doi:10.1107/S090744490001115X ]

Structural analysis of non-crystalline macromolecules: the ribosome

E. V. Orlova

Synopsis: A description of the main steps of the structural analysis of non-crystalline biological macromolecules using cryo-electron microscopy is given in this paper.

Online October 2000

 

Acta Cryst. (2000). D56, 1259-1269  [ doi:10.1107/S0907444900011252 ]

Assessment of electron crystallographic data obtained from two-dimensional crystals of biological specimens

V. M. Unger

Synopsis: Electron crystallographic data from 2D crystals are being generated and published at an accelerating pace. However, unlike in X-ray crystallography, there are no standardized criteria in electron crystallography that can help investigators and reviewers alike to judge the reliability of electron crystallographic data. This article discusses some of the relevant issues and intends to serve as a platform for further discussion.

Online October 2000

 

Acta Cryst. (2000). D56, 1270-1277  [ doi:10.1107/S0907444900009549 ]

Resolution measurement in structures derived from single particles

N. Grigorieff

Synopsis: Analytical expressions are derived and computer simulations are used to assess the accuracy of common resolution measures for protein structures derived from images of single molecules of complexes. It is concluded that the alignment of images is accompanied by a correlation of noise, and that this correlation leads to erroneous resolution measurements.

Online October 2000

 

Acta Cryst. (2000). D56, 1278-1287  [ doi:10.1107/S0907444900010817 ]

Supplanting crystallography or supplementing microscopy? A combined approach to the study of an enveloped virus

E. J. Mancini and S. D. Fuller

Synopsis: The complementarity of X-ray and cryo-electron microscopy results is illustrated in the determination and interpretation of the structure of an enveloped virus at 9 Å resolution.

Online October 2000

 

Acta Cryst. (2000). D56, 1288-1303  [ doi:10.1107/S0907444900009574 ]

Low-resolution phase information in multiple-wavelength anomalous solvent contrast variation experiments

W. Shepard, R. Kahn, M. Ramin and R. Fourme

Synopsis: A complete account of the MASC method is given from the basic theory and experimental considerations through to the phasing of the macromolecular envelope at low resolution.

Online October 2000

 

Acta Cryst. (2000). D56, 1304-1311  [ doi:10.1107/S0907444900008982 ]

In-house low-resolution X-ray crystallography

G. Evans, P. Roversi and G. Bricogne

Synopsis: Modifications to a standard in-house X-ray diffraction camera (Elliot-GX13/300 mm MAR IP) are presented which allow the measurement of very low resolution diffraction intensities (>200 Å).

Online October 2000

 

Acta Cryst. (2000). D56, 1312-1315  [ doi:10.1107/S0907444900008970 ]

The oversampling phasing method

J. Miao, J. Kirz and D. Sayre

Synopsis: Sampling the diffraction pattern of a finite specimen more finely than the Nyquist frequency corresponds to surrounding the electron density of the specimen with a no-density region. This no-density region can be used to retrieve the phase information directly from the diffraction pattern.

Online October 2000

 

Acta Cryst. (2000). D56, 1316-1323  [ doi:10.1107/S0907444900008490 ]

Modelling prior distributions of atoms for macromolecular refinement and completion

P. Roversi, E. Blanc, C. Vonrhein, G. Evans and G. Bricogne

Synopsis: Homographic exponential models give a compact representation of probability distributions for the missing part of a macromolecular crystal structure and for the bulk solvent. These distributions are used in the maximum-likelihood refinement and maximum-entropy completion of partial structures.

PDB reference: 1lvy

Online October 2000

 

Acta Cryst. (2000). D56, 1324-1331  [ doi:10.1107/S0907444900010283 ]

Low-resolution phase extension using wavelet analysis

P. Main and J. Wilson

Synopsis: Predicted values for wavelet coefficients are used to extend phases from 10 Å to around 6-7 Å.

Online October 2000

 

Acta Cryst. (2000). D56, 1332-1340  [ doi:10.1107/S0907444900010908 ]

Docking structures of domains into maps from cryo-electron microscopy using local correlation

A. M. Roseman

Synopsis: Atomic models of large macromolecular complexes can be built by docking the atomic structures of components into cryo-EM maps. A procedure based on local real-space correlation is presented and verified by docking the domains from the crystal structure of GroEL into a cryo-EM map of the oligomer.

Online October 2000

 

Acta Cryst. (2000). D56, 1341-1349  [ doi:10.1107/S0907444900009562 ]

Fitting atomic models into electron-microscopy maps

M. G. Rossmann

Synopsis: Techniques are described and examples are given for the interpretation of lower resolution cryo-EM results by using higher, near atomic resolution crystallographic results of component structures.

Online October 2000

 

Acta Cryst. (2000). D56, 1350-1357  [ doi:10.1107/S0907444900009410 ]

When two into one won't go: fitting in the presence of steric hindrance and partial occupancy

E. Thouvenin and E. Hewat

Synopsis: Two techniques of fitting X-ray to EM data in the presence of steric hindrance are presented and applied to a rotavirus-Fab complex. As the X-ray structures of the Fab and the Fab bound to a viral protein are known, this is a good test case.

Online October 2000