Dear Colleagues,
The Cold Spring Harbor Macromolecular Crystallography course will take place October 13-29th this year (pleased see below for more details). This comprehensive course is an outstanding place to learn both the theoretical and practical aspects of macromolecular crystallography. There are extensive lectures and practical sessions from world recognized experts in crystallization, data collection, data processing, structure solution, refinement, and validation. The goal of the course is for researchers who have had some exposure to structural biology to become experts in crystallography. This is an experience in macromolecular crystallography learning that cannot be found anywhere else, and the student/teacher ratio is often 1:1.
Please follow the link below to the course web site. In particular, please note the information about the various fellowships, scholarships, and stipends that are available.
If anyone has any questions please send me an e-mail, and we will be happy to answer all queries.
Paul Adams
<https://r20.rs6.net/tn.jsp?f=001fnNri6rmFxDJaH0HgFMkV8PNwKevLhjwrpcpWrfCqoq…>
<https://r20.rs6.net/tn.jsp?f=001fnNri6rmFxDJaH0HgFMkV8PNwKevLhjwrpcpWrfCqoq…>
Macromolecular Crystallography <https://r20.rs6.net/tn.jsp?f=001fnNri6rmFxDJaH0HgFMkV8PNwKevLhjwrpcpWrfCqoq…>
October 13 - 29, 2024
Applications Due: July 15
Instructors
Paul Adams, Lawrence Berkeley National Laboratory
Dorothee Liebschner, Lawrence Berkeley National Laboratory
Janet Newman, UNSW, Australia
James Pflugrath, Rigaku Americas Corporation (ret.), Texas
Co-Instructor
Tom Peat, UNSW, Australia
Topics Covered
Basic Diffraction Theory
Structure Presentation
Coordinate Deposition
Structure Validation
Model Building and Refinement
Electron Density Maps Improvement
Using Predicted Models in Structure Solution and Completion
Protein Structure Prediction
Structure Solution by Experimental Phasing Methods (SAD, MAD, MIR, and others) and Molecular Replacement
Data Collection and Processing
Synchrotron X-ray Sources and Optics
Crystallization (Proteins, Nucleic Acids, Complexes and Membrane Proteins)
For further information and to apply please visit the Macromolecular Crystallography course website. <https://r20.rs6.net/tn.jsp?f=001fnNri6rmFxDJaH0HgFMkV8PNwKevLhjwrpcpWrfCqoq…>
Cold Spring Harbor Laboratory - Meetings & Courses | 1 Bungtown Road, Cold Spring Harbor, NY 11724
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Paul Adams (he/him/his)
Associate Laboratory Director for Biosciences, LBL (https://biosciences.lbl.gov)
Principal Investigator, Computational Crystallography Initiative, LBL (http://cci.lbl.gov)
Vice President for Technology, the Joint BioEnergy Institute (http://www.jbei.org)
Principal Investigator, ALS-ENABLE, Advanced Light Source (http://als-enable.lbl.gov)
Laboratory Research Manager, ENIGMA Science Focus Area (http://enigma.lbl.gov)
Adjunct Professor, Department of Bioengineering, UC Berkeley (http://bioeng.berkeley.edu)
Member of the Graduate Group in Comparative Biochemistry, UC Berkeley (http://compbiochem.berkeley.edu)
Building 91, Room 410
Building 978, Room 4126
Tel: 1-510-486-4225
http://cci.lbl.gov/paul
ORCID: 0000-0001-9333-8219
Lawrence Berkeley Laboratory
1 Cyclotron Road
BLDG 91R0183
Berkeley, CA 94720, USA.
Executive Assistant: Michael Espinosa [ MEEspinosa(a)lbl.gov ][ 1-510-333-6788 ]
Phenix Consortium: Ashley Dawn [ AshleyDawn(a)lbl.gov ][ 1-510-486-5455 ]
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Hello,
I ran resolve_cryoem for solvent flattening and obtained a ccp4 map that behaves like a mask both in Coot and Chimera. the histogram is just a single line and the dimensions are different from my original map, even though in a second run I used restore_full_size = true in a second run.
To be clear, my original map has 480^3 dimensions, and the output one is 125x140x224, which boxes my protein but I can't see the inside of the map.
I guess there is something I didn't understand. Can you please help me?
All the best,
Valerie
Valérie Biou, Ph.D. valerie.biou(a)ibpc.fr
Laboratoire de Biologie Physico-Chimique des Protéines Membranaires
umr7099.ibpc.fr <http://umr7099.ibpc.fr/>
UMR 7099 CNRS/Univ. Paris-Cité
Institut de Biologie Physico-Chimique
13 rue Pierre et Marie Curie
75005 Paris - France
Tel : +33 (0)1 5841 5099
